Delta2D Labels

Delta2D Labels
for Project 'Demonstration'

Report created by DECODON with Delta2D, Thu Nov 25 12:00:00 CET 2010. An overview of the reports is available in the Report Index.

Project Name		Demonstration
Project Creation Date		Wed Feb 22 19:00:00 CET 2006
Author		Decodon
Description		Delta2D demonstration project. A time-course experiment with three samples separated in duplicate. We thank Falko Hochgräfe for the gel images
Use Internal Standard		no
Pool		C:\Users\DECODON\.Delta2D\demopool

Labels

Table shows label data for all labels on gel image 'control_01'. If a label is annotating a detected spot, this spot is shown as well.

Label	Pi/MW Estimation	Spot	GenoList	Uniprot	AureoList
Name	X	Y	Pi	MW	ID	Gene Size (bp)	Isoelectric Point	Molecular Weight (Da)	Protein Size (aa)	Function	Accession	Amino Acids	Function	Gene name	Gene Ontology	Isoelectric Point	Keywords	Molecular Weight	NCBI Taxonomy	Organism	Original label name	Protein name	Query text	References	Sequence	Title	Uniprot entry	Gene Size (bp)	Isoelectric Point	Molecular Weight (Da)	Protein Size (aa)
AhpC	876	689	4.07	23560	13405	561	4.283	20482.3	187		P80239	187	Directly reduces organic hydroperoxides in its reduced dithiol form.	ahpC	F:peroxidase activity [GO:0004601] F:peroxiredoxin activity [GO:0051920] P:cell redox homeostasis [GO:0045454] P:oxidation reduction [GO:0055114] P:response to stress [GO:0006950]	4.2224	Antioxidant Complete proteome Direct protein sequencing Disulfide bond Oxidoreductase Peroxidase Redox-active center Stress response	20627.06	1423	Bacillus subtilis	AhpC	Alkyl hydroperoxide reductase subunit C	AhpC	4 references	MSLIGKEVLPFEAKAFKNGEFIDVTNEDLKGQWSVFCFYPADFSFVCPTELEDLQEQYAA LKELGVEVYSVSTDTHFVHKGWHDSSEKISKITYAMIGDPSQTISRNFDVLDEETGLADR GTFIIDPDGVIQTVEINAGGIGRDASNLVNKVKAAQYVRQNPGEVCPAKWEEGGETLTPS LDLVGKI	AHPC_BACSU	P80239	570	4.6566	20976.6	189
AhpF	711	271	4.67	74015	13694	1527	4.705	54705.4	509		P42974	509	Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).	ahpF	C:plasma membrane [GO:0005886] F:electron carrier activity [GO:0009055] F:FAD or FADH2 binding [GO:0050660] F:NAD or NADH binding [GO:0051287] F:NADH dehydrogenase activity [GO:0003954] F:protein disulfide oxidoreductase activity [GO:0015035] P:cell redox homeostasis [GO:0045454] P:electron transport chain [GO:0022900] P:transport [GO:0006810]	4.6273	Cell membrane Complete proteome Direct protein sequencing Disulfide bond Electron transport FAD Flavoprotein Membrane NAD Oxidoreductase Redox-active center Transport Ubiquinone	54874.24	1423	Bacillus subtilis	AhpF	NADH dehydrogenase	AhpF	4 references	MVLDANIKAQLNQYMQLIENDIVLKVSAGEDDTSKDMLALVDELASMSSKISVEKAELNR TPSFSVNRVGEDTGVTFAGIPLGHEFTSLVLALLQVSGRPPKVDQKVIDQVKKISGEYHF ESYISLTCHNCPDVVQALNMMSVLNPNITHTMIDGAAYKAEVESKNIMAVPTVYLNGESF GSGRMTLEEILAKMGSGTDASEFADKEPFDVLVVGGGPAGASAAIYTARKGIRTGVVAER FGGQVLDTMSIENFISVKATEGPKLAASLEEHVKEYDIDVMNLQRAKRLEKKDLFELELE NGAVLKSKTVILSTGARWRNVNVPGEQEFKNKGVAYCPHCDGPLFEGKDVAVIGGGNSGI EAAIDLAGIVNHVTVLEFAPELKADEVLQKRLYSLPNVTVVKNAQTKEITGDQSVNGITY VDRETGEEKHVELQGVFVQIGLVPNTEWLEGTVERNRMGEIIVDKHGATSVPGLFAAGDC TDSAYNQIIISMGSGATAALGAFDYLIRN	DHNA_BACSU	P42974	1524	4.4183	54707.6	507
AroA	450	398	5.51	53230	13758	1074	5.341	39382.2	358		P39912	358		aroA	F:3-deoxy-7-phosphoheptulonate synthase activity [GO:0003849] F:aldehyde-lyase activity [GO:0016832] F:chorismate mutase activity [GO:0004106] P:aromatic amino acid family biosynthetic pro... [GO:0009073]	5.3543	Amino-acid biosynthesis Aromatic amino acid biosynthesis Complete proteome Isomerase Multifunctional enzyme Phosphoprotein Transferase	39539.34	1423	Bacillus subtilis	AroA	Protein AroA(G)	AroA	4 references	MSNTELELLRQKADELNLQILKLINERGNVVKEIGKAKEAQGVNRFDPVRERTMLNNIIE NNDGPFENSTIQHIFKEIFKAGLELQEEDHSKALLVSRKKKPEDTIVDIKGEKIGDGQQR FIVGPCAVESYEQVAEVAAAAKKQGIKILRGGAFKPRTSPYDFQGLGVEGLQILKRVADE FDLAVISEIVTPAHIEEALDYIDVIQIGARNMQNFELLKAAGAVKKPVLLKRGLAATISE FINAAEYIMSQGNDQIILCERGIRTYETATRNTLDISAVPILKQETHLPVFVDVTHSTGR RDLLLPTAKAALAIGADGVMAEVHPDPSVALSDSAQQMAIPEFEKWLNELKPMVKVNA	AROG_BACSU	P39912	1299	4.8402	47068.1	432
CysK	384	535	5.71	37252	13286	924	5.492	32666.0	308		P37887	308	Catalyzes the conversion of O-acetylserine to cysteine. Also acts as a sensor of cysteine availability in the signal transduction pathway modulating CymR activity. When cysteine is present, the pool of O-acetylserine (OAS) is low, which leads to the formation of a CymR-CysK complex and transcriptional repression of the CymR regulon occurs. In the absence of cysteine, the OAS pool is high and the CymR-CysK complex is mostly dissociated, leading to a faster dissociation of CymR from its DNA targets and the lifting of CymR-dependent repression.	cysK	F:cysteine synthase activity [GO:0004124] F:pyridoxal phosphate binding [GO:0030170] F:transferase activity [GO:0016740] P:cysteine biosynthetic process from serine [GO:0006535]	5.512	Amino-acid biosynthesis Complete proteome Cysteine biosynthesis Direct protein sequencing Pyridoxal phosphate Transferase	32819.5	1423	Bacillus subtilis	CysK	Cysteine synthase	CysK	7 references	MVRVANSITELIGNTPIVKLNRLADENSADVYLKLEYMNPGSSVKDRIGLAMIEAAEKEG KLKAGNTIIEPTSGNTGIGLAMVAAAKGLKAILVMPDTMSMERRNLLRAYGAELVLTPGA EGMKGAIKKAEELAEKHGYFVPQQFNNPSNPEIHRQTTGKEIVEQFGDDQLDAFVAGIGT GGTITGAGEVLKEAYPSIKIYAVEPSDSPVLSGGKPGPHKIQGIGAGFVPDILNTEVYDE IFPVKNEEAFEYARRAAREEGILGGISSGAAIYAALQVAKKLGKGKKVLAIIPSNGERYL STPLYQFD	CYSK_BACSU	P37887	933	5.1289	32975.6	310
DnaK	751	178	4.55	96792	13886	1833	4.571	65825.8	611		P17820	611	Acts as a chaperone (By similarity).	dnaK	F:ATP binding [GO:0005524] F:unfolded protein binding [GO:0051082] P:protein folding [GO:0006457] P:response to stress [GO:0006950]	4.4949	3D-structure ATP-binding Chaperone Complete proteome Direct protein sequencing Nucleotide-binding Phosphoprotein Stress response	66001.93	1423	Bacillus subtilis	DnaK	Chaperone protein dnaK	DnaK	7 references	MSKVIGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAFKNGERQVGEVAKRQSITN PNTIMSIKRHMGTDYKVEIEGKDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYF NDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDKTDEDQTILVYDLGGGTFDVSILE LGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVSEFKKENGIDLSKDKMALQRLKDAAEKAK KDLSGVSSTQISLPFITAGEAGPLHLELTLTRAKFEELSSHLVERTMGPVRQALQDAGLS ASEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAIQGGVITGDVKDVV LLDVTPLSLGIETMGGVFTKLIDRNTTIPTSKSQVFSTAADNQTAVDIHVLQGERPMSAD NKTLGRFQLTDIPPAPRGVPQIEVSFDIDKNGIVNVRAKDLGTGKEQNITIKSSSGLSDE EIERMVKEAEENADADAKKKEEIEVRNEADQLVFQTEKTLKDLEGKVDEEQVKKANDAKD ALKAAIEKNEFEEIKAKKDELQTIVQELSMKLYEEAAKAQQAQGGANAEGKADDNVVDAE YEEVNDDQNKK	DNAK_BACSU	P17820	1833	4.385	66361.1	610
Dps	815	783	4.26	16672	13438	435	4.444	16450.9	145		P80879	145		dps	F:ferric iron binding [GO:0008199] F:oxidoreductase activity [GO:0016491] P:cellular iron ion homeostasis [GO:0006879] P:oxidation reduction [GO:0055114] P:response to stress [GO:0006950]	4.3681	Complete proteome Direct protein sequencing Stress response	16593.69	1423	Bacillus subtilis	Dps	General stress protein 20U	Dps	3 references	MSEQLIQAVNKQVANWTVMYVKLHNYHWYVKGKDFFTLHEKFEELYNETATYIDDLAERL LALNGKPIATMKESLETASVKEAAGNETAEQMVQSVYDDFTVIAEELKNGMDLADEVGDE TTGDMLLAIHQNIEKHNWMLKAYLG	G20U_BACSU	P80879	444	4.2946	16691.6	147
Dps	778	804	4.37	15214	13444	435	4.444	16450.9	145		P80879	145		dps	F:ferric iron binding [GO:0008199] F:oxidoreductase activity [GO:0016491] P:cellular iron ion homeostasis [GO:0006879] P:oxidation reduction [GO:0055114] P:response to stress [GO:0006950]	4.3681	Complete proteome Direct protein sequencing Stress response	16593.69	1423	Bacillus subtilis	Dps	General stress protein 20U	Dps	3 references	MSEQLIQAVNKQVANWTVMYVKLHNYHWYVKGKDFFTLHEKFEELYNETATYIDDLAERL LALNGKPIATMKESLETASVKEAAGNETAEQMVQSVYDDFTVIAEELKNGMDLADEVGDE TTGDMLLAIHQNIEKHNWMLKAYLG	G20U_BACSU	P80879	444	4.2946	16691.6	147
EF-G	708	131	4.70	113380	13850	0	0.0	0.0	0		P80868	692	This protein promotes the GTP-dependent translocation of the nascent protein chain from the A-site to the P-site of the ribosome.	fusA	C:cytoplasm [GO:0005737] F:GTP binding [GO:0005525] F:GTPase activity [GO:0003924] F:translation elongation factor activity [GO:0003746]	4.5137	Complete proteome Cytoplasm Direct protein sequencing Elongation factor GTP-binding Nucleotide-binding Phosphoprotein Protein biosynthesis	76616.39	1423	Bacillus subtilis	EF-G	Elongation factor G	EF-G	6 references	MAREFSLEKTRNIGIMAHIDAGKTTTTERILFYTGRIHKIGETHEGASQMDWMEQEQERG ITITSAATTAQWKGYRVNIIDTPGHVDFTVEVERSLRVLDGAVAVLDAQSGVEPQTETVW RQATTYGVPRIVFVNKMDKIGADFLYSVGTLRDRLQANAHAIQLPIGAEDNFEGIIDLVE NVAYFYEDDLGTRSDAKEIPEEYKEQAEELRNSLIEAVCELDEELMDKYLEGEEITIDEL KAGIRKGTLNVEFYPVLVGSAFKNKGVQLVLDAVLDYLPAPTDVAAIKGTRPDTNEEIER HSSDEEPFSALAFKVMTDPYVGKLTFFRVYSGTLDSGSYVKNSTKGKRERVGRILQMHAN SREEISTVYAGDIAAAVGLKDTTTGDTLCDEKDLVILESMEFPEPVIDVAIEPKSKADQD KMGIALAKLAEEDPTFRTQTNPETGQTIISGMGELHLDIIVDRMKREFKVEANVGAPQVA YRETFRTGAKVEGKFVRQSGGRGQFGHVWIEFEPNEEGAGFEFENAIVGGVVPREYIPAV QAGLEDALENGVLAGFPLIDIKAKLFDGSYHDVDSNEMAFKVAASMALKNAVSKCNPVLL EPIMKVEVVIPEEYMGDIMGDITSRRGRVEGMEARGNAQVVRAMVPLAEMFGYATALRSN TQGRGTFTMHMDHYEEVPKSVAEEIIKKNKGE	EFG_BACSU	P80868	0	0.0	0.0	0
EF-Ts	589	467	5.04	44607	13220	0	0.0	0.0	0		P80700	293	Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.	tsf	C:cytoplasm [GO:0005737] F:translation elongation factor activity [GO:0003746]	4.9006	Complete proteome Cytoplasm Direct protein sequencing Elongation factor Phosphoprotein Protein biosynthesis	32353.67	1423	Bacillus subtilis	EF-Ts	Elongation factor Ts	EF-Ts	3 references	MAITAQQVKELREKTGAGMMDCKKALTETDGDMDKAIDLLREKGIAKAAKKADRIAAEGS TLIKTDGNKGVILEVNSETDFVAKNEGFKELLNTLADHLLANTPADVEEAMGQKMENGST VEEYITSAVAKIGEKITLRRFTVLTKDDSSAFGAYLHMGGRIGVLTVLNGTTDEETAKDI AMHVAAVNPRYISRDQVSEEETNHERQILTQQALQEGKPENIVAKMVEGRLNKFFEEICL LDQAFVKNPDEKVKQVIAAKNATVQTFVRYEVGEGIEKRQENFAEEVMNQVKK	EFTS_BACSU	P80700	0	0.0	0.0	0
EF-Tu	680	317	4.76	65568	13712	0	0.0	0.0	0		P33166	396	This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.	tuf	C:cytoplasm [GO:0005737] F:GTP binding [GO:0005525] F:GTPase activity [GO:0003924] F:translation elongation factor activity [GO:0003746]	4.6468	Complete proteome Cytoplasm Elongation factor GTP-binding Nucleotide-binding Protein biosynthesis	43593.15	1423	Bacillus subtilis	EF-Tu	Elongation factor Tu	EF-Tu	3 references	MAKEKFDRSKSHANIGTIGHVDHGKTTLTAAITTVLHKKSGKGTAMAYDQIDGAPEERER GITISTAHVEYETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREH ILLSKNVGVPYIVVFLNKCDMVDDEELLELVEMEVRDLLSEYDFPGDDVPVVKGSALKAL EGDAEWEAKIFELMDAVDEYIPTPERDTEKPFMMPVEDVFSITGRGTVATGRVERGQVKV GDEVEIIGLQEENKKTTVTGVEMFRKLLDYAEAGDNIGALLRGVSREEIQRGQVLAKPGT ITPHSKFKAEVYVLSKEEGGRHTPFFSNYRPQFYFRTTDVTGIIHLPEGVEMVMPGDNTE MNVELISTIAIEEGTRFSIREGGRTVGSGVVSTITE	EFTU_BACSU	P33166	0	0.0	0.0	0
Eno	772	340	4.46	61779	13721	1290	4.485	46417.9	430		P37869	430	Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis (By similarity).	eno	C:cell surface [GO:0009986] C:extracellular region [GO:0005576] C:phosphopyruvate hydratase complex [GO:0000015] F:magnesium ion binding [GO:0000287] F:phosphopyruvate hydratase activity [GO:0004634] P:glycolysis [GO:0006096] P:sporulation resulting in formation of a cel... [GO:0030435]	4.4037	Complete proteome Cytoplasm Direct protein sequencing Glycolysis Lyase Magnesium Metal-binding Phosphoprotein Secreted Sporulation	46581.26	1423	Bacillus subtilis	Eno	Enolase	Eno	6 references	MPYIVDVYAREVLDSRGNPTVEVEVYTETGAFGRALVPSGASTGEYEAVELRDGDKDRYL GKGVLTAVNNVNEIIAPELLGFDVTEQNAIDQLLIELDGTENKGKLGANAILGVSMACAR AAADFLQIPLYQYLGGFNSKTLPVPMMNIVNGGEHADNNVDIQEFMIMPVGAPNFREALR MGAQIFHSLKSVLSAKGLNTAVGDEGGFAPNLGSNEEALQTIVEAIEKAGFKPGEEVKLA MDAASSEFYNKEDGKYHLSGEGVVKTSAEMVDWYEELVSKYPIISIEDGLDENDWEGHKL LTERLGKKVQLVGDDLFVTNTKKLSEGIKNGVGNSILIKVNQIGTLTETFDAIEMAKRAG YTAVISHRSGETEDSTIADIAVATNAGQIKTGAPSRTDRVAKYNQLLRIEDQLAETAQYH GINSFYNLNK	ENO_BACSU	P37869	1305	4.2796	47116.8	434
GapA	544	371	5.20	57058	13947	1005	5.033	35676.2	335	catabolic enzyme	D5MXM7	340		BSU6633_04772	F:carbohydrate binding [GO:0030246] F:transcription regulator activity [GO:0030528]	5.8427		37410.06	703612	Bacillus subtilis subsp. spizizenii ATCC 6633	GapA		GapA	1 references	MNQLIQAQKKLLPDLLLVMQKRFEILQYIRLTEPIGRRSLSASLGISERVLRGEVQFLKE QNLVDIKTNGMTLTEEGYELLSVLEDTMKDVLGLTLLEKTLKERLNLKDAIIVSGDSDQS PWVKKEMGRAAVACMKKRFSGKNIVAVTGGTTIEAVAEMMTPDSKNRELLFVPARGGLGE DVKNQANTICAHMAEKASGTYRLLFVPGQLSQGAYSSIIEEPSVKEVLNTIKSASMLVHG IGEAKTMAQRRNTPLEDLKKIDDNDAVTEAFGYYFNVDGEVVHKVHSVGMQLDDIDAIPD IIAVAGGSSKAEAIEAYFKKPRNTVLVTDEGAAKKLLRDE	D5MXM7_BACSU	D5MXM7	0	0.0	0.0	0
GlnA	629	297	4.93	69075	13070	1332	4.874	50113.3	444		P94459	3603	This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Pro, Gln and Tyr as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Tyr residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains.	ppsD	F:acyl carrier activity [GO:0000036] F:cofactor binding [GO:0048037] F:ligase activity [GO:0016874] F:phosphopantetheine binding [GO:0031177] F:transferase activity [GO:0016740] P:antibiotic biosynthetic process [GO:0017000]	5.5	Antibiotic biosynthesis Complete proteome Leucine-rich repeat Multifunctional enzyme Phosphopantetheine Repeat Transferase	406811.2	1423	Bacillus subtilis	GlnA	Plipastatin synthase subunit D	GlnA	5 references	MTKANSIQDIYPLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGKVNPQFFQNSINALVER HDIFRTIFISQNVSSPQQVVLRERNVIVLEEDITHLNEAEQSQFIEQWKEKDRDRGFHLQ KDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLHIYASYVNASPITLEPVQP YGKYIKWLMEQDKEQAVSYWDHYLSGHEQQTVLPKQKKTKGKSRQEHVTFSFSKEESSRL SELAAREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRPAEIEGIEHMVGLFINTMP VRVQGAKTPFLQLIKDMQKDRLAAEAYSYHPLYEIQSRSAVKQGLIDHILVFENYPVQQE IQMLNKQEHASDLFQIHNFTVADETNYSFYLMVAPGEEIHIKMNYDAEQHDRSFVLSVKE HLLNAVSQILNNPNLPPEEIDITTDTEKRQLIGEITDQTPVYETIHAMFEKQAEKTPDAH AVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAI VPVDPHYPADRIRYILHDCGCSHVVSQAHLPSSLEDNYIITHPEDIESKVDGSNIKSVNN ADDLLYMIYTSGTTGKPKGVQFEHRNMANLLKFEYTHSGIDFEADVLQFATPSFDVCYQE IFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQTNIVFLPTAFIKMIFSERELANSFPDG VKHLIAAGEQLMISDLFQDVLRKRGIHLHNHYGPSETHVVSTYTIHPGDPIPELPPIGKP IGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPDVIMYRT GDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHE LCAYYCSVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALPEPDASIS GNPYTAPRNLLEAKLSQLFEDVLKNGHIGIQDNFFDNGGHSLKATVLMSRIAKEFHVQVS LKDIFAHPTVEGLALIIREAEQNLYAAIEPAEKRDTYPVSSAQKRIYVLQQLDEGVAYNM PAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSGADDEPVQRIHTEVPFTLSKETTIE GFVRPFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLYANRQLKP LRIQYKDYAVWQQKFKKGDSYQKQETYWQQQFSGDLPILELPTDKRRPAERQFIGGKVTF QLDKEITARIKRLAHKNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPHADLEAVL GMFVNTLALRTRPAGNKTFEEFLKEVRQTALEAYEHQDYPFEELVDKLGVQREMSRNPLF DTTLVLQNMEQQKLKMNDVQLQWNDLEHPISKFDISLYVTEHDSELFCQFEYSTALFEKE TIQRWASLFTTLVEHTAASPETELDNIPILTKEEERDFIESCHLFEETGYSMNQTLHYAL EQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLG IYGILKAGGAYLPIDPDYPEERISFLLEDSGTNILLLQSAGLHVPEFTGEIVYLNQTNSG LAHRLSNPNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIM HKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVPSMLHAF LEHIKYRSVPIKTNRLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAFFD CPPHEKLERIPIGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEER FLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVR EAAVTVRTDSGEPELCAYVEGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDR NALPAPGGAADAETYTAPRNVTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKATALVS RITKEFDVQVPLKDVFAHPTVEGLATVIREGTDSPYEAIKPAEKQETYPVSSAQKRIYVL QQLEDGGTGYNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFEQDEGGDPVQRIHDE VPFTLQTTVLGARTEQEAAAAFIKPFDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGV SVNILIQEFGELYNNRKLPALRIQYKDYAVWQEGFKTGDAYKMQEAYWLKQLEGELPVLD LPADHARPPVRSFAGDKVSFTLEPEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQE DIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQNYP FEELVDKLELTRDMSRNPVFDAMLVVQNNDYEPLHLHDLQMKPAQVSHLVSKFDLTLQAS EGDGNIHFLFEYSTALFEKTTIERWASHLTNVLSIIGKNPKVTLNHIDILTQEERHQLLN EFNTGQANQYGVQTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGV KPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMTINEA DLGVLADFEGEILTIESVEEDDKSPLPQMSSAHHLAYIIYTSGTTGRPKGVMVEHKGIAN TLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIKHQL SRQRITHMIIVPVLYRALLDVVQPEDVKTLRVVTLAGEAADRELIARSLAICPHTELANE YGPTENSVATTVMRHMEKQAYVSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLAR GYVNLPELTERAFTQNPFKPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKE IESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLSTNAVRSELQNKLPVFMHPAFI EKLDSLPLSPNGKLDRGALPKPVYNHEGERPFLPPSSKMEQILADIWKEVLGAEKIGTAD SFFELGGDSIKALQVSARLHRIGKQMAVKDLFSHPTIQELAAYIRDSDTSSSQAAVEGDV QWSPVQKWFLSQDIKEKHHFNQSVMLHRSTSVQEDALRKTLKAITCHHDALRMVFTQNEQ GKWDQYNRPLSHSDDALYGLQMIDLSAPDGTDGNRPYEPLIKRHVLDIQQKMDLKNGPLL QAGLFHTIDGDFLFLSAHHLVVDGISWRVLLEDLALGYRQAAGGEDIKLPPKTSSFKAYA KKLSDYAESQQLMKQLKYWREAEEYQTEALPFDQIDGTRAHEGQRSTISFTLNDKETAAL LKDANSAYNTDTQDMLLASVILALRHWTNQSAFKLSLEGHGREDVLKGIDVSRTIGWFTA IYPLLIKLNADLPDSEESMVHVLKTTKDTLRRVPDKGFGYGVIKYLTPPGKKDINFTGAP EISFNYLGQFESGRTAEVPEEDAFSFSPLGAGGDISTTWNREQSLDISAIAAEGKLTVNM TYDNARFQRKTIEQLSETCRQFLLQLIEHCQNKSETEKTISDFDDQELTEDALQEIADML SFH	PPSD_BACSU	P94459	1341	4.8414	50854.6	446
GroEL	748	213	4.56	87080	13911	1632	4.531	57251.9	544		P28598	544	Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (By similarity).	groL	C:cytoplasm [GO:0005737] F:ATP binding [GO:0005524] F:protein binding [GO:0005515] P:protein folding [GO:0006457] P:response to stress [GO:0006950]	4.4284	ATP-binding Chaperone Complete proteome Cytoplasm Direct protein sequencing Nucleotide-binding Stress response	57424.41	1423	Bacillus subtilis	GroEL	60 kDa chaperonin	GroEL	8 references	MAKEIKFSEEARRAMLRGVDALADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIE LEDAFENMGAKLVAEVASKTNDVAGDGTTTATVLAQAMIREGLKNVTAGANPVGVRKGME QAVAVAIENLKEISKPIEGKESIAQVAAISAADEEVGSLIAEAMERVGNDGVITIEESKG FTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDNPYILITDKKITNIQEILPVLEQVVQ QGKPLLLIAEDVEGEALATLVVNKLRGTFNAVAVKAPGFGDRRKAMLEDIAVLTGGEVIT EDLGLDLKSTQIAQLGRASKVVVTKENTTIVEGAGETDKISARVTQIRAQVEETTSEFDR EKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDALNSTRAAVEEGIVSGGGTALVNV YNKVAAVEAEGDAQTGINIVLRALEEPIRQIAHNAGLEGSVIVERLKNEEIGVGFNAATG EWVNMIEKGIVDPTKVTRSALQNAASVAAMFLTTEAVVADKPEENGGGAGMPDMGGMGGM GGMM	CH60_BACSU	P28598	1617	4.2854	57572.0	538
GspA	584	513	5.05	39513	13630	858	5.089	33368.4	286		P25148	286		gspA	F:transferase activity, transferring glycosyl... [GO:0016757] P:response to stress [GO:0006950]	5.1076	Complete proteome Direct protein sequencing Stress response	33521.9	1423	Bacillus subtilis	GspA	General stress protein A	GspA	5 references	MRKDEIMHIVSCADDNYARHLGGMFVSLLTNMDQEREVKLYVIDGGIKPDNKKRLEETTL KFGVPIEFLEVDTNMYEHAVESSHITKAAYYRISIPDLIKDESIKRMIYIDCDALVLEDI SKLWDLDIAPYTVAAVEDAGQHERLKEMNVTDTGKYFNSGIMIIDFESWRKQNITEKVIN FINEHPDEDFLVLHDQDALNAILYDQWYELHPRWNAQTYIMLKLKTPSTLLGRKQYNETR ENPAIVHFCGGEKPWNSNTKHPYRDEYFHYMSYTKWNTIGNPAINQ	GSPA_BACSU	P25148	0	0.0	0.0	0
GspA	551	512	5.16	39653	13629	858	5.089	33368.4	286		P25148	286		gspA	F:transferase activity, transferring glycosyl... [GO:0016757] P:response to stress [GO:0006950]	5.1076	Complete proteome Direct protein sequencing Stress response	33521.9	1423	Bacillus subtilis	GspA	General stress protein A	GspA	5 references	MRKDEIMHIVSCADDNYARHLGGMFVSLLTNMDQEREVKLYVIDGGIKPDNKKRLEETTL KFGVPIEFLEVDTNMYEHAVESSHITKAAYYRISIPDLIKDESIKRMIYIDCDALVLEDI SKLWDLDIAPYTVAAVEDAGQHERLKEMNVTDTGKYFNSGIMIIDFESWRKQNITEKVIN FINEHPDEDFLVLHDQDALNAILYDQWYELHPRWNAQTYIMLKLKTPSTLLGRKQYNETR ENPAIVHFCGGEKPWNSNTKHPYRDEYFHYMSYTKWNTIGNPAINQ	GSPA_BACSU	P25148	0	0.0	0.0	0
GtaB	612	514	4.96	39402	13627	876	4.913	32917.4	292	glucosylation of teichoic acid	Q05852	292	Catalyzes the formation of UDP-glucose from glucose-1-phosphate and UTP. This is an intermediate step in the biosynthesis of diglucosyl-diacylglycerol (Glc2-DAG), i.e. the predominant glycolipid found in B.subtilis membrane, which is also used as a membrane anchor for lipoteichoic acid (LTA). Has a role in the biosynthesis of all phosphate-containing envelope polymers, since UDP-glucose serves as a glucosyl donor not only for the biosynthesis of LTA but also for wall teichoic acids (WTAs). Is required for biofilm formation. This is likely due to another role of UDP-glucose, which might also act as a metabolic signal regulating biofilm formation or may be involved in some unknown biosynthetic pathway essential for biofilm formation, e.g. the synthesis of an exopolysaccharide.	gtaB	F:UTP:glucose-1-phosphate uridylyltransferase... [GO:0003983] P:biosynthetic process [GO:0009058] P:response to stress [GO:0006950] P:UDP-glucose metabolic process [GO:0006011]	4.8218	Carbohydrate metabolism Complete proteome Direct protein sequencing Nucleotidyltransferase Stress response Transferase	33069.93	1423	Bacillus subtilis	GtaB	UTP--glucose-1-phosphate uridylyltransferase	GtaB	6 references	MKKVRKAIIPAAGLGTRFLPATKAMPKEMLPIVDKPTIQYIIEEAVEAGIEDIIIVTGKS KRAIEDHFDYSPELERNLEEKGKTELLEKVKKASNLADIHYIRQKEPKGLGHAVWCARNF IGDEPFAVLLGDDIVQAETPGLRQLMDEYEKTLSSIIGVQQVPEEETHRYGIIDPLTSEG RRYQVKNFVEKPPKGTAPSNLAILGRYVFTPEIFMYLEEQQVGAGGEIQLTDAIQKLNEI QRVFAYDFEGKRYDVGEKLGFITTTLEFAMQDKELRDQLVPFMEGLLNKEEI	GTAB_BACSU	Q05852	867	5.1766	32451.1	288
Hag	662	420	4.81	50346	13751	912	4.782	32472.0	304		P02968	304	Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.	hag	C:bacterial-type flagellum filament [GO:0009420] C:cell wall [GO:0005618] C:extracellular region [GO:0005576] F:structural molecule activity [GO:0005198] P:ciliary or flagellar motility [GO:0001539]	4.7354	Bacterial flagellum Cell wall Complete proteome Direct protein sequencing Secreted	32626.22	1423	Bacillus subtilis	Hag	Flagellin	Hag	9 references	MRINHNIAALNTLNRLSSNNSASQKNMEKLSSGLRINRAGDDAAGLAISEKMRGQIRGLE MASKNSQDGISLIQTAEGALTETHAILQRVRELVVQAGNTGTQDKATDLQSIQDEISALT DEIDGISNRTEFNGKKLLDGTYKVDTATPANQKNLVFQIGANATQQISVNIEDMGADALG IKEADGSIAALHSVNDLDVTKFADNAADTADIGFDAQLKVVDEAINQVSSQRAKLGAVQN RLEHTINNLSASGENLTAAESRIRDVDMAKEMSEFTKNNILSQASQAMLAQANQQPQNVL QLLR	FLA_BACSU	P02968	0	0.0	0.0	0
Icd	664	358	4.81	58976	13729	1269	4.833	46255.0	423		P39126	423		icd	F:isocitrate dehydrogenase (NADP+) activity [GO:0004450] F:magnesium ion binding [GO:0000287] F:NAD or NADH binding [GO:0051287] P:glyoxylate cycle [GO:0006097] P:oxidation reduction [GO:0055114] P:tricarboxylic acid cycle [GO:0006099]	4.7445	3D-structure Complete proteome Glyoxylate bypass Magnesium Manganese Metal-binding NADP Oxidoreductase Tricarboxylic acid cycle	46417.64	1423	Bacillus subtilis	Icd	Isocitrate dehydrogenase [NADP]	Icd	5 references	MAQGEKITVSNGVLNVPNNPIIPFIEGDGTGPDIWNAASKVLEAAVEKAYKGEKKITWKE VYAGEKAYNKTGEWLPAETLDVIREYFIAIKGPLTTPVGGGIRSLNVALRQELDLFVCLR PVRYFTGVPSPVKRPEDTDMVIFRENTEDIYAGIEYAKGSEEVQKLISFLQNELNVNKIR FPETSGIGIKPVSEEGTSRLVRAAIDYAIEHGRKSVTLVHKGNIMKFTEGAFKNWGYELA EKEYGDKVFTWAQYDRIAEEQGKDAANKAQSEAEAAGKIIIKDSIADIFLQQILTRPNEF DVVATMNLNGDYISDALAAQVGGIGIAPGANINYETGHAIFEATHGTAPKYAGLDKVNPS SVILSGVLLLEHLGWNEAADLVIKSMEKTIASKVVTYDFARLMDGATEVKCSEFGEELIK NMD	IDH_BACSU	P39126	0	0.0	0.0	0
IlvC	433	407	5.56	52047	13760	1026	5.37	37302.2	342		P37253	342		ilvC	F:coenzyme binding [GO:0050662] F:ketol-acid reductoisomerase activity [GO:0004455] P:branched chain family amino acid biosynthet... [GO:0009082] P:oxidation reduction [GO:0055114]	5.4597	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Complete proteome Direct protein sequencing NADP Oxidoreductase	37457.57	1423	Bacillus subtilis	IlvC	Ketol-acid reductoisomerase	IlvC	4 references	MVKVYYNGDIKENVLAGKTVAVIGYGSQGHAHALNLKESGVDVIVGVRQGKSFTQAQEDG HKVFSVKEAAAQAEIIMVLLPDEQQQKVYEAEIKDELTAGKSLVFAHGFNVHFHQIVPPA DVDVFLVAPKGPGHLVRRTYEQGAGVPALFAIYQDVTGEARDKALAYAKGIGGARAGVLE TTFKEETETDLFGEQAVLCGGLSALVKAGFETLTEAGYQPELAYFECLHELKLIVDLMYE EGLAGMRYSISDTAQWGDFVSGPRVVDAKVKESMKEVLKDIQNGTFAKEWIVENQVNRPR FNAINASENEHQIEVVGRKLREMMPFVKQGKKKEAVVSVAQN	ILVC_BACSU	P37253	1005	4.9518	37013.8	334
KatA	203	259	6.34	76501	13035	1449	6.151	54566.7	483		P26901	483	Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.	katA	C:cytoplasm [GO:0005737] F:catalase activity [GO:0004096] F:heme binding [GO:0020037] P:hydrogen peroxide catabolic process [GO:0042744] P:oxidation reduction [GO:0055114]	6.5182	Complete proteome Cytoplasm Direct protein sequencing Heme Hydrogen peroxide Iron Metal-binding Oxidoreductase Peroxidase	54791.13	1423	Bacillus subtilis	KatA	Vegetative catalase	KatA	7 references	MSSNKLTTSWGAPVGDNQNSMTAGSRGPTLIQDVHLLEKLAHFNRERVPERVVHAKGAGA HGYFEVTNDVTKYTKAAFLSEVGKRTPLFIRFSTVAGELGSADTVRDPRGFAVKFYTEEG NYDIVGNNTPVFFIRDAIKFPDFIHTQKRDPKTHLKNPTAVWDFWSLSPESLHQVTILMS DRGIPATLRHMHGFGSHTFKWTNAEGEGVWIKYHFKTEQGVKNLDVNTAAKIAGENPDYH TEDLFNAIENGDYPAWKLYVQIMPLEDANTYRFDPFDVTKVWSQKDYPLIEVGRMVLDRN PENYFAEVEQATFSPGTLVPGIDVSPDKMLQGRLFAYHDAHRYRVGANHQALPINRARNK VNNYQRDGQMRFDDNGGGSVYYEPNSFGGPKESPEDKQAAYPVQGIADSVSYDHYDHYTQ AGDLYRLMSEDERTRLVENIVNAMKPVEKEEIKLRQIEHFYKADPEYGKRVAEGLGLPIK KDS	CATA_BACSU	P26901	1524	5.1325	58612.0	507
Mdh	691	446	4.71	47065	13196	936	4.727	33489.7	312		P49814	312	Catalyzes the reversible oxidation of malate to oxaloacetate (By similarity).	mdh	F:binding [GO:0005488] F:L-malate dehydrogenase activity [GO:0030060] P:glycolysis [GO:0006096] P:malate metabolic process [GO:0006108] P:oxidation reduction [GO:0055114] P:tricarboxylic acid cycle [GO:0006099]	4.644	Complete proteome Direct protein sequencing NAD Oxidoreductase Phosphoprotein Tricarboxylic acid cycle	33643.43	1423	Bacillus subtilis	Mdh	Malate dehydrogenase	Mdh	6 references	MGNTRKKVSVIGAGFTGATTAFLIAQKELADVVLVDIPQLENPTKGKALDMLEASPVQGF DAKITGTSNYEDTAGSDIVVITAGIARKPGMSRDDLVSTNEKIMRSVTQEIVKYSPDSII VVLTNPVDAMTYAVYKESGFPKERVIGQSGVLDTARFRTFVAEELNLSVKDVTGFVLGGH GDDMVPLVRYSYAGGIPLETLIPKERIDAIVERTRKGGGEIVNLLGNGSAYYAPAASLTE MVEAILKDQRRVLPTIAYLEGEYGYEGIYLGVPTIVGGNGLEQIIELELTDYERAQLNKS VESVKNVMKVLS	MDH_BACSU	P49814	0	0.0	0.0	0
Pgk	674	348	4.78	60512	13723	1182	4.768	42030.1	394		P40924	394		pgk	C:cytoplasm [GO:0005737] F:ATP binding [GO:0005524] F:phosphoglycerate kinase activity [GO:0004618] P:glycolysis [GO:0006096]	4.7055	ATP-binding Complete proteome Cytoplasm Direct protein sequencing Glycolysis Kinase Nucleotide-binding Phosphoprotein Transferase	42190.17	1423	Bacillus subtilis	Pgk	Phosphoglycerate kinase	Pgk	4 references	MNKKTLKDIDVKGKVVFCRVDFNVPMKDGEVTDDTRIRAALPTIKHLADQGAKVLLASHL GRPKGEVVEELRLTPVAARLGELLGKEVKKADEAYGDAVKAQISEMKDGDVLVLENVRFY PGEEKNDPELAKAFAELADVYVNDAFGAAHRAHASTAGIAEHLPAVAGFLMEKELDVLGK AVSNPDRPFTAIIGGAKVKDKIGVIESLLDKVDNLIIGGGLAYTFVKALGYEVGKSLLEE DKIELAKSFMDRAKEKGVNFYMPEDVLVADDFSNDANVKIVPISEIPSDLEAIDIGTKTR ETYADVIKNSKLVVWNGPMGVFEIDLFAQGTKAVAEALAEAKDTYSVIGGGDSAAAVEKF GLADKMSHISTGGGASLEFMEGKELPGVAALNDK	PGK_BACSU	P40924	1191	4.9614	42601.6	396
PtsH	676	997	4.68	3585	13610	264	4.584	9051.3	88	transfers phosphate from enzyme I to specific enzymes II/III permeases; mediates carbon catabolite repression (CCR)	P08877	88	General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the permease (enzymes II/III).	ptsH	C:cytoplasm [GO:0005737] F:kinase activity [GO:0016301] F:sugar:hydrogen symporter activity [GO:0005351] P:phosphoenolpyruvate-dependent sugar phospho... [GO:0009401] P:regulation of transcription [GO:0045449] P:transcription [GO:0006350]	4.5185	3D-structure Complete proteome Cytoplasm Direct protein sequencing Kinase Phosphoprotein Phosphotransferase system Sugar transport Transcription Transcription regulation Transferase Transport	9189.33	1423	Bacillus subtilis	PtsH	Phosphocarrier protein HPr	PtsH	13 references	MAQKTFKVTADSGIHARPATVLVQTASKYDADVNLEYNGKTVNLKSIMGVMSLGIAKGAE ITISASGADENDALNALEETMKSEGLGE	PTHP_BACSU	P08877	267	4.2677	9495.7	88
RsbW	870	775	4.08	17194	13432	480	4.285	17849.6	160	negative regulation of sigma-B-dependent gene expression; phosphorylation of RsbV	P17904	160	Negative regulator of sigma-B activity. Phosphorylates and inactivates its specific antagonist protein, rsbV. Upon phosphorylation of rsbV, rsbW is released and binds to sigma-B, thereby blocking its ability to form an RNA polymerase holoenzyme (E-sigma-B).	rsbW	F:ATP binding [GO:0005524] F:protein serine/threonine kinase activity [GO:0004674] F:sigma factor antagonist activity [GO:0016989] P:negative regulation of transcription, DNA-d... [GO:0045892] P:protein phosphorylation [GO:0006468] P:response to stress [GO:0006950]	4.231	ATP-binding Complete proteome Direct protein sequencing Kinase Nucleotide-binding Stress response Transferase	17992.95	1423	Bacillus subtilis	RsbW	Serine-protein kinase rsbW	RsbW	9 references	MKNNADYIEMKVPAQPEYVGIIRLTLSGVASRMGYTYDEIEDLKIAVSEACTNAVQHAYK EDKNGEVSIRFGVFEDRLEVIVADEGDSFDFDQKQQDLGPYTPSHTVDQLSEGGLGLYLM ETLMDEVRVQNHSGVTVAMTKYLNGERVDHDTTIKNYETN	RSBW_BACSU	P17904	480	4.4501	17921.2	159
SodA	608	665	4.95	25484	13575	606	5.203	22428.8	202		P54375	202	Destroys radicals which are normally produced within the cells and which are toxic to biological systems.	sodA	C:cytoplasm [GO:0005737] F:metal ion binding [GO:0046872] F:superoxide dismutase activity [GO:0004784] P:oxidation reduction [GO:0055114] P:response to stress [GO:0006950] P:superoxide metabolic process [GO:0006801]	5.0627	3D-structure Complete proteome Cytoplasm Direct protein sequencing Manganese Metal-binding Oxidoreductase Phosphoprotein Stress response	22489.88	1423	Bacillus subtilis	SodA	Superoxide dismutase [Mn]	SodA	8 references	MAYELPELPYAYDALEPHIDKETMTIHHTKHHNTYVTNLNKAVEGNTALANKSVEELVAD LDSVPENIRTAVRNNGGGHANHKLFWTLLSPNGGGEPTGALAEEINSVFGSFDKFKEQFA AAAAGRFGSGWAWLVVNNGKLEITSTPNQDSPLSEGKTPILGLDVWEHAYYLNYQNRRPD YISAFWNVVNWDEVARLYSEAK	SODM_BACSU	P54375	600	4.8565	22711.3	199
Spot_01	149	320	6.51	65138	13091
Spot_02	153	461	6.48	45263	13222
YdbD	644	513	4.86	39485	13628	819	4.858	30105.8	273	unknown	D4G5B9	273		ydbD	F:oxidoreductase activity [GO:0016491] F:transition metal ion binding [GO:0046914] P:oxidation reduction [GO:0055114]	4.7875		30316.31	645657	Bacillus subtilis subsp. natto BEST195	YdbD		YdbD	1 references	MFKHTKMLQHPAKPDRPDPLFAKKMQEILGGQFGEISVAMQYLFQGWNTRGNEKYKDLLM DTATEELGHVEMIATMIARLLEDAPLDQQEKAAEDPVIGSILGGMNPHHAIVSGLGAMPE SSTGVPWSGGYIVASGNLLADFRANLNAESQGRLQVARLFEMTDDKGVKDMLSFLLARDT MHQNQWLAAIKELEAQEGPVVPGTFPKALEKQEFSHQLINFSEGEESAQQNWLNEKAPDG EAFEYVKEAKTFGEKPELKPTPPFVHNTLPGRE	D4G5B9_BACNA	D4G5B9	0	0.0	0.0	0
YtxH	565	743	5.08	19457	13588	456	5.107	16542.7	152	unknown	P40780	151		ytxH		5.0722	Complete proteome	16554.55	1423	Bacillus subtilis	YtxH	Uncharacterized protein ytxH	YtxH	3 references	MSKDGINSKDFLIGTLIGGIIGATTALFLAPKSGKELRDDLGSQAVALRDKTDKMTADAK EKGTQYVSIAKDKTSNITQLVADQSGQIMNKVKDLRDRSKSDKTDSSTAMQDMREEAMQA ADETKDQVLQTKEDVKDELKDAQKQAEQLNR	YTXH_BACSU	P40780	0	0.0	0.0	0
YvyD	518	622	5.25	29100	13563	567	5.184	21833.7	189	unknown	P28368	189		yvyD	F:binding [GO:0005488] P:primary metabolic process [GO:0044238]	5.1806	Complete proteome	21979.65	1423	Bacillus subtilis	YvyD	Uncharacterized protein yvyD	YvyD	4 references	MNYNIRGENIEVTPALKDHVERKIGKLERYFDHSVDADVNVNLKFYNDKESKVEVTIPMT DLALRSEVHNEDMYNAIDLATNKLERQIRKHKTKVNRKFREQGSPKYLLANGLGSDTDIA VQDDIEEEESLDIVRQKRFNLKPMDSEEAILQMNMLGHNFFVFTNAETNLTNVVYRRNDG KYGLIEPTE	YVYD_BACSU	P28368	0	0.0	0.0	0

Label

Pi/MW Estimation

Spot

GenoList

Uniprot

AureoList

Name

Gene Size (bp)

Isoelectric Point

Molecular Weight (Da)

Protein Size (aa)

Function

Accession

Amino Acids

Function

Gene name

Gene Ontology

Isoelectric Point

Keywords

Molecular Weight

NCBI Taxonomy

Organism

Original label name

Protein name

Query text

References

Sequence

Title

Uniprot entry

Gene Size (bp)

Isoelectric Point

Molecular Weight (Da)

Protein Size (aa)

AhpC

876

689

4.07

23560

13405

561

4.283

20482.3

187

P80239

187

Directly reduces organic hydroperoxides in its reduced dithiol form.

ahpC

F:peroxidase activity [GO:0004601]
F:peroxiredoxin activity [GO:0051920]
P:cell redox homeostasis [GO:0045454]
P:oxidation reduction [GO:0055114]
P:response to stress [GO:0006950]

4.2224

20627.06

1423

Bacillus subtilis

AhpC

Alkyl hydroperoxide reductase subunit C

AhpC

4 references

MSLIGKEVLPFEAKAFKNGEFIDVTNEDLKGQWSVFCFYPADFSFVCPTELEDLQEQYAA LKELGVEVYSVSTDTHFVHKGWHDSSEKISKITYAMIGDPSQTISRNFDVLDEETGLADR GTFIIDPDGVIQTVEINAGGIGRDASNLVNKVKAAQYVRQNPGEVCPAKWEEGGETLTPS LDLVGKI

AHPC_BACSU

P80239

570

4.6566

20976.6

189

AhpF

711

271

4.67

74015

13694

1527

4.705

54705.4

509

P42974

509

Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).

ahpF

C:plasma membrane [GO:0005886]
F:electron carrier activity [GO:0009055]
F:FAD or FADH2 binding [GO:0050660]
F:NAD or NADH binding [GO:0051287]
F:NADH dehydrogenase activity [GO:0003954]
F:protein disulfide oxidoreductase activity [GO:0015035]
P:cell redox homeostasis [GO:0045454]
P:electron transport chain [GO:0022900]
P:transport [GO:0006810]

4.6273

54874.24

1423

Bacillus subtilis

AhpF

NADH dehydrogenase

AhpF

4 references

MVLDANIKAQLNQYMQLIENDIVLKVSAGEDDTSKDMLALVDELASMSSKISVEKAELNR TPSFSVNRVGEDTGVTFAGIPLGHEFTSLVLALLQVSGRPPKVDQKVIDQVKKISGEYHF ESYISLTCHNCPDVVQALNMMSVLNPNITHTMIDGAAYKAEVESKNIMAVPTVYLNGESF GSGRMTLEEILAKMGSGTDASEFADKEPFDVLVVGGGPAGASAAIYTARKGIRTGVVAER FGGQVLDTMSIENFISVKATEGPKLAASLEEHVKEYDIDVMNLQRAKRLEKKDLFELELE NGAVLKSKTVILSTGARWRNVNVPGEQEFKNKGVAYCPHCDGPLFEGKDVAVIGGGNSGI EAAIDLAGIVNHVTVLEFAPELKADEVLQKRLYSLPNVTVVKNAQTKEITGDQSVNGITY VDRETGEEKHVELQGVFVQIGLVPNTEWLEGTVERNRMGEIIVDKHGATSVPGLFAAGDC TDSAYNQIIISMGSGATAALGAFDYLIRN

DHNA_BACSU

P42974

1524

4.4183

54707.6

507

AroA

450

398

5.51

53230

13758

1074

5.341

39382.2

358

P39912

358

aroA

F:3-deoxy-7-phosphoheptulonate synthase activity [GO:0003849]
F:aldehyde-lyase activity [GO:0016832]
F:chorismate mutase activity [GO:0004106]
P:aromatic amino acid family biosynthetic pro... [GO:0009073]

5.3543

39539.34

1423

Bacillus subtilis

AroA

Protein AroA(G)

AroA

4 references

MSNTELELLRQKADELNLQILKLINERGNVVKEIGKAKEAQGVNRFDPVRERTMLNNIIE NNDGPFENSTIQHIFKEIFKAGLELQEEDHSKALLVSRKKKPEDTIVDIKGEKIGDGQQR FIVGPCAVESYEQVAEVAAAAKKQGIKILRGGAFKPRTSPYDFQGLGVEGLQILKRVADE FDLAVISEIVTPAHIEEALDYIDVIQIGARNMQNFELLKAAGAVKKPVLLKRGLAATISE FINAAEYIMSQGNDQIILCERGIRTYETATRNTLDISAVPILKQETHLPVFVDVTHSTGR RDLLLPTAKAALAIGADGVMAEVHPDPSVALSDSAQQMAIPEFEKWLNELKPMVKVNA

AROG_BACSU

P39912

1299

4.8402

47068.1

432

CysK

384

535

5.71

37252

13286

924

5.492

32666.0

308

P37887

308

Catalyzes the conversion of O-acetylserine to cysteine. Also acts as a sensor of cysteine availability in the signal transduction pathway modulating CymR activity. When cysteine is present, the pool of O-acetylserine (OAS) is low, which leads to the formation of a CymR-CysK complex and transcriptional repression of the CymR regulon occurs. In the absence of cysteine, the OAS pool is high and the CymR-CysK complex is mostly dissociated, leading to a faster dissociation of CymR from its DNA targets and the lifting of CymR-dependent repression.

cysK

F:cysteine synthase activity [GO:0004124]
F:pyridoxal phosphate binding [GO:0030170]
F:transferase activity [GO:0016740]
P:cysteine biosynthetic process from serine [GO:0006535]

5.512

32819.5

1423

Bacillus subtilis

CysK

Cysteine synthase

CysK

7 references

MVRVANSITELIGNTPIVKLNRLADENSADVYLKLEYMNPGSSVKDRIGLAMIEAAEKEG KLKAGNTIIEPTSGNTGIGLAMVAAAKGLKAILVMPDTMSMERRNLLRAYGAELVLTPGA EGMKGAIKKAEELAEKHGYFVPQQFNNPSNPEIHRQTTGKEIVEQFGDDQLDAFVAGIGT GGTITGAGEVLKEAYPSIKIYAVEPSDSPVLSGGKPGPHKIQGIGAGFVPDILNTEVYDE IFPVKNEEAFEYARRAAREEGILGGISSGAAIYAALQVAKKLGKGKKVLAIIPSNGERYL STPLYQFD

CYSK_BACSU

P37887

933

5.1289

32975.6

310

DnaK

751

178

4.55

96792

13886

1833

4.571

65825.8

611

P17820

611

Acts as a chaperone (By similarity).

dnaK

F:ATP binding [GO:0005524]
F:unfolded protein binding [GO:0051082]
P:protein folding [GO:0006457]
P:response to stress [GO:0006950]

4.4949

66001.93

1423

Bacillus subtilis

DnaK

Chaperone protein dnaK

DnaK

7 references

MSKVIGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAFKNGERQVGEVAKRQSITN PNTIMSIKRHMGTDYKVEIEGKDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYF NDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDKTDEDQTILVYDLGGGTFDVSILE LGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVSEFKKENGIDLSKDKMALQRLKDAAEKAK KDLSGVSSTQISLPFITAGEAGPLHLELTLTRAKFEELSSHLVERTMGPVRQALQDAGLS ASEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAIQGGVITGDVKDVV LLDVTPLSLGIETMGGVFTKLIDRNTTIPTSKSQVFSTAADNQTAVDIHVLQGERPMSAD NKTLGRFQLTDIPPAPRGVPQIEVSFDIDKNGIVNVRAKDLGTGKEQNITIKSSSGLSDE EIERMVKEAEENADADAKKKEEIEVRNEADQLVFQTEKTLKDLEGKVDEEQVKKANDAKD ALKAAIEKNEFEEIKAKKDELQTIVQELSMKLYEEAAKAQQAQGGANAEGKADDNVVDAE YEEVNDDQNKK

DNAK_BACSU

P17820

1833

4.385

66361.1

610

Dps

815

783

4.26

16672

13438

435

4.444

16450.9

145

P80879

145

dps

F:ferric iron binding [GO:0008199]
F:oxidoreductase activity [GO:0016491]
P:cellular iron ion homeostasis [GO:0006879]
P:oxidation reduction [GO:0055114]
P:response to stress [GO:0006950]

4.3681

16593.69

1423

Bacillus subtilis

Dps

General stress protein 20U

Dps

3 references

MSEQLIQAVNKQVANWTVMYVKLHNYHWYVKGKDFFTLHEKFEELYNETATYIDDLAERL LALNGKPIATMKESLETASVKEAAGNETAEQMVQSVYDDFTVIAEELKNGMDLADEVGDE TTGDMLLAIHQNIEKHNWMLKAYLG

G20U_BACSU

P80879

444

4.2946

16691.6

147

Dps

778

804

4.37

15214

13444

435

4.444

16450.9

145

P80879

145

dps

F:ferric iron binding [GO:0008199]
F:oxidoreductase activity [GO:0016491]
P:cellular iron ion homeostasis [GO:0006879]
P:oxidation reduction [GO:0055114]
P:response to stress [GO:0006950]

4.3681

16593.69

1423

Bacillus subtilis

Dps

General stress protein 20U

Dps

3 references

MSEQLIQAVNKQVANWTVMYVKLHNYHWYVKGKDFFTLHEKFEELYNETATYIDDLAERL LALNGKPIATMKESLETASVKEAAGNETAEQMVQSVYDDFTVIAEELKNGMDLADEVGDE TTGDMLLAIHQNIEKHNWMLKAYLG

G20U_BACSU

P80879

444

4.2946

16691.6

147

EF-G

708

131

4.70

113380

13850

0.0

P80868

692

This protein promotes the GTP-dependent translocation of the nascent protein chain from the A-site to the P-site of the ribosome.

fusA

C:cytoplasm [GO:0005737]
F:GTP binding [GO:0005525]
F:GTPase activity [GO:0003924]
F:translation elongation factor activity [GO:0003746]

4.5137

76616.39

1423

Bacillus subtilis

EF-G

Elongation factor G

EF-G

6 references

MAREFSLEKTRNIGIMAHIDAGKTTTTERILFYTGRIHKIGETHEGASQMDWMEQEQERG ITITSAATTAQWKGYRVNIIDTPGHVDFTVEVERSLRVLDGAVAVLDAQSGVEPQTETVW RQATTYGVPRIVFVNKMDKIGADFLYSVGTLRDRLQANAHAIQLPIGAEDNFEGIIDLVE NVAYFYEDDLGTRSDAKEIPEEYKEQAEELRNSLIEAVCELDEELMDKYLEGEEITIDEL KAGIRKGTLNVEFYPVLVGSAFKNKGVQLVLDAVLDYLPAPTDVAAIKGTRPDTNEEIER HSSDEEPFSALAFKVMTDPYVGKLTFFRVYSGTLDSGSYVKNSTKGKRERVGRILQMHAN SREEISTVYAGDIAAAVGLKDTTTGDTLCDEKDLVILESMEFPEPVIDVAIEPKSKADQD KMGIALAKLAEEDPTFRTQTNPETGQTIISGMGELHLDIIVDRMKREFKVEANVGAPQVA YRETFRTGAKVEGKFVRQSGGRGQFGHVWIEFEPNEEGAGFEFENAIVGGVVPREYIPAV QAGLEDALENGVLAGFPLIDIKAKLFDGSYHDVDSNEMAFKVAASMALKNAVSKCNPVLL EPIMKVEVVIPEEYMGDIMGDITSRRGRVEGMEARGNAQVVRAMVPLAEMFGYATALRSN TQGRGTFTMHMDHYEEVPKSVAEEIIKKNKGE

EFG_BACSU

P80868

0.0

EF-Ts

589

467

5.04

44607

13220

0.0

P80700

293

Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.

tsf

C:cytoplasm [GO:0005737]
F:translation elongation factor activity [GO:0003746]

4.9006

32353.67

1423

Bacillus subtilis

EF-Ts

Elongation factor Ts

EF-Ts

3 references

MAITAQQVKELREKTGAGMMDCKKALTETDGDMDKAIDLLREKGIAKAAKKADRIAAEGS TLIKTDGNKGVILEVNSETDFVAKNEGFKELLNTLADHLLANTPADVEEAMGQKMENGST VEEYITSAVAKIGEKITLRRFTVLTKDDSSAFGAYLHMGGRIGVLTVLNGTTDEETAKDI AMHVAAVNPRYISRDQVSEEETNHERQILTQQALQEGKPENIVAKMVEGRLNKFFEEICL LDQAFVKNPDEKVKQVIAAKNATVQTFVRYEVGEGIEKRQENFAEEVMNQVKK

EFTS_BACSU

P80700

0.0

EF-Tu

680

317

4.76

65568

13712

0.0

P33166

396

This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.

tuf

C:cytoplasm [GO:0005737]
F:GTP binding [GO:0005525]
F:GTPase activity [GO:0003924]
F:translation elongation factor activity [GO:0003746]

4.6468

43593.15

1423

Bacillus subtilis

EF-Tu

Elongation factor Tu

EF-Tu

3 references

MAKEKFDRSKSHANIGTIGHVDHGKTTLTAAITTVLHKKSGKGTAMAYDQIDGAPEERER GITISTAHVEYETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREH ILLSKNVGVPYIVVFLNKCDMVDDEELLELVEMEVRDLLSEYDFPGDDVPVVKGSALKAL EGDAEWEAKIFELMDAVDEYIPTPERDTEKPFMMPVEDVFSITGRGTVATGRVERGQVKV GDEVEIIGLQEENKKTTVTGVEMFRKLLDYAEAGDNIGALLRGVSREEIQRGQVLAKPGT ITPHSKFKAEVYVLSKEEGGRHTPFFSNYRPQFYFRTTDVTGIIHLPEGVEMVMPGDNTE MNVELISTIAIEEGTRFSIREGGRTVGSGVVSTITE

EFTU_BACSU

P33166

0.0

Eno

772

340

4.46

61779

13721

1290

4.485

46417.9

430

P37869

430

Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis (By similarity).

eno

C:cell surface [GO:0009986]
C:extracellular region [GO:0005576]
C:phosphopyruvate hydratase complex [GO:0000015]
F:magnesium ion binding [GO:0000287]
F:phosphopyruvate hydratase activity [GO:0004634]
P:glycolysis [GO:0006096]
P:sporulation resulting in formation of a cel... [GO:0030435]

4.4037

46581.26

1423

Bacillus subtilis

Eno

Enolase

Eno

6 references

MPYIVDVYAREVLDSRGNPTVEVEVYTETGAFGRALVPSGASTGEYEAVELRDGDKDRYL GKGVLTAVNNVNEIIAPELLGFDVTEQNAIDQLLIELDGTENKGKLGANAILGVSMACAR AAADFLQIPLYQYLGGFNSKTLPVPMMNIVNGGEHADNNVDIQEFMIMPVGAPNFREALR MGAQIFHSLKSVLSAKGLNTAVGDEGGFAPNLGSNEEALQTIVEAIEKAGFKPGEEVKLA MDAASSEFYNKEDGKYHLSGEGVVKTSAEMVDWYEELVSKYPIISIEDGLDENDWEGHKL LTERLGKKVQLVGDDLFVTNTKKLSEGIKNGVGNSILIKVNQIGTLTETFDAIEMAKRAG YTAVISHRSGETEDSTIADIAVATNAGQIKTGAPSRTDRVAKYNQLLRIEDQLAETAQYH GINSFYNLNK

ENO_BACSU

P37869

1305

4.2796

47116.8

434

GapA

544

371

5.20

57058

13947

1005

5.033

35676.2

335

catabolic enzyme

D5MXM7

340

BSU6633_04772

F:carbohydrate binding [GO:0030246]
F:transcription regulator activity [GO:0030528]

5.8427

37410.06

703612

Bacillus subtilis subsp. spizizenii ATCC 6633

GapA

1 references

MNQLIQAQKKLLPDLLLVMQKRFEILQYIRLTEPIGRRSLSASLGISERVLRGEVQFLKE QNLVDIKTNGMTLTEEGYELLSVLEDTMKDVLGLTLLEKTLKERLNLKDAIIVSGDSDQS PWVKKEMGRAAVACMKKRFSGKNIVAVTGGTTIEAVAEMMTPDSKNRELLFVPARGGLGE DVKNQANTICAHMAEKASGTYRLLFVPGQLSQGAYSSIIEEPSVKEVLNTIKSASMLVHG IGEAKTMAQRRNTPLEDLKKIDDNDAVTEAFGYYFNVDGEVVHKVHSVGMQLDDIDAIPD IIAVAGGSSKAEAIEAYFKKPRNTVLVTDEGAAKKLLRDE

D5MXM7_BACSU

D5MXM7

0.0

GlnA

629

297

4.93

69075

13070

1332

4.874

50113.3

444

P94459

3603

This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Pro, Gln and Tyr as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Tyr residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains.

ppsD

F:acyl carrier activity [GO:0000036]
F:cofactor binding [GO:0048037]
F:ligase activity [GO:0016874]
F:phosphopantetheine binding [GO:0031177]
F:transferase activity [GO:0016740]
P:antibiotic biosynthetic process [GO:0017000]

5.5

406811.2

1423

Bacillus subtilis

GlnA

Plipastatin synthase subunit D

GlnA

5 references

MTKANSIQDIYPLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGKVNPQFFQNSINALVER HDIFRTIFISQNVSSPQQVVLRERNVIVLEEDITHLNEAEQSQFIEQWKEKDRDRGFHLQ KDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLHIYASYVNASPITLEPVQP YGKYIKWLMEQDKEQAVSYWDHYLSGHEQQTVLPKQKKTKGKSRQEHVTFSFSKEESSRL SELAAREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRPAEIEGIEHMVGLFINTMP VRVQGAKTPFLQLIKDMQKDRLAAEAYSYHPLYEIQSRSAVKQGLIDHILVFENYPVQQE IQMLNKQEHASDLFQIHNFTVADETNYSFYLMVAPGEEIHIKMNYDAEQHDRSFVLSVKE HLLNAVSQILNNPNLPPEEIDITTDTEKRQLIGEITDQTPVYETIHAMFEKQAEKTPDAH AVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAI VPVDPHYPADRIRYILHDCGCSHVVSQAHLPSSLEDNYIITHPEDIESKVDGSNIKSVNN ADDLLYMIYTSGTTGKPKGVQFEHRNMANLLKFEYTHSGIDFEADVLQFATPSFDVCYQE IFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQTNIVFLPTAFIKMIFSERELANSFPDG VKHLIAAGEQLMISDLFQDVLRKRGIHLHNHYGPSETHVVSTYTIHPGDPIPELPPIGKP IGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPDVIMYRT GDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHE LCAYYCSVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALPEPDASIS GNPYTAPRNLLEAKLSQLFEDVLKNGHIGIQDNFFDNGGHSLKATVLMSRIAKEFHVQVS LKDIFAHPTVEGLALIIREAEQNLYAAIEPAEKRDTYPVSSAQKRIYVLQQLDEGVAYNM PAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSGADDEPVQRIHTEVPFTLSKETTIE GFVRPFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLYANRQLKP LRIQYKDYAVWQQKFKKGDSYQKQETYWQQQFSGDLPILELPTDKRRPAERQFIGGKVTF QLDKEITARIKRLAHKNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPHADLEAVL GMFVNTLALRTRPAGNKTFEEFLKEVRQTALEAYEHQDYPFEELVDKLGVQREMSRNPLF DTTLVLQNMEQQKLKMNDVQLQWNDLEHPISKFDISLYVTEHDSELFCQFEYSTALFEKE TIQRWASLFTTLVEHTAASPETELDNIPILTKEEERDFIESCHLFEETGYSMNQTLHYAL EQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLG IYGILKAGGAYLPIDPDYPEERISFLLEDSGTNILLLQSAGLHVPEFTGEIVYLNQTNSG LAHRLSNPNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIM HKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVPSMLHAF LEHIKYRSVPIKTNRLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAFFD CPPHEKLERIPIGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEER FLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVR EAAVTVRTDSGEPELCAYVEGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDR NALPAPGGAADAETYTAPRNVTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKATALVS RITKEFDVQVPLKDVFAHPTVEGLATVIREGTDSPYEAIKPAEKQETYPVSSAQKRIYVL QQLEDGGTGYNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFEQDEGGDPVQRIHDE VPFTLQTTVLGARTEQEAAAAFIKPFDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGV SVNILIQEFGELYNNRKLPALRIQYKDYAVWQEGFKTGDAYKMQEAYWLKQLEGELPVLD LPADHARPPVRSFAGDKVSFTLEPEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQE DIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQNYP FEELVDKLELTRDMSRNPVFDAMLVVQNNDYEPLHLHDLQMKPAQVSHLVSKFDLTLQAS EGDGNIHFLFEYSTALFEKTTIERWASHLTNVLSIIGKNPKVTLNHIDILTQEERHQLLN EFNTGQANQYGVQTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGV KPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMTINEA DLGVLADFEGEILTIESVEEDDKSPLPQMSSAHHLAYIIYTSGTTGRPKGVMVEHKGIAN TLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIKHQL SRQRITHMIIVPVLYRALLDVVQPEDVKTLRVVTLAGEAADRELIARSLAICPHTELANE YGPTENSVATTVMRHMEKQAYVSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLAR GYVNLPELTERAFTQNPFKPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKE IESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLSTNAVRSELQNKLPVFMHPAFI EKLDSLPLSPNGKLDRGALPKPVYNHEGERPFLPPSSKMEQILADIWKEVLGAEKIGTAD SFFELGGDSIKALQVSARLHRIGKQMAVKDLFSHPTIQELAAYIRDSDTSSSQAAVEGDV QWSPVQKWFLSQDIKEKHHFNQSVMLHRSTSVQEDALRKTLKAITCHHDALRMVFTQNEQ GKWDQYNRPLSHSDDALYGLQMIDLSAPDGTDGNRPYEPLIKRHVLDIQQKMDLKNGPLL QAGLFHTIDGDFLFLSAHHLVVDGISWRVLLEDLALGYRQAAGGEDIKLPPKTSSFKAYA KKLSDYAESQQLMKQLKYWREAEEYQTEALPFDQIDGTRAHEGQRSTISFTLNDKETAAL LKDANSAYNTDTQDMLLASVILALRHWTNQSAFKLSLEGHGREDVLKGIDVSRTIGWFTA IYPLLIKLNADLPDSEESMVHVLKTTKDTLRRVPDKGFGYGVIKYLTPPGKKDINFTGAP EISFNYLGQFESGRTAEVPEEDAFSFSPLGAGGDISTTWNREQSLDISAIAAEGKLTVNM TYDNARFQRKTIEQLSETCRQFLLQLIEHCQNKSETEKTISDFDDQELTEDALQEIADML SFH

PPSD_BACSU

P94459

1341

4.8414

50854.6

446

GroEL

748

213

4.56

87080

13911

1632

4.531

57251.9

544

P28598

544

Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (By similarity).

groL

C:cytoplasm [GO:0005737]
F:ATP binding [GO:0005524]
F:protein binding [GO:0005515]
P:protein folding [GO:0006457]
P:response to stress [GO:0006950]

4.4284

57424.41

1423

Bacillus subtilis

GroEL

60 kDa chaperonin

GroEL

8 references

MAKEIKFSEEARRAMLRGVDALADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIE LEDAFENMGAKLVAEVASKTNDVAGDGTTTATVLAQAMIREGLKNVTAGANPVGVRKGME QAVAVAIENLKEISKPIEGKESIAQVAAISAADEEVGSLIAEAMERVGNDGVITIEESKG FTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDNPYILITDKKITNIQEILPVLEQVVQ QGKPLLLIAEDVEGEALATLVVNKLRGTFNAVAVKAPGFGDRRKAMLEDIAVLTGGEVIT EDLGLDLKSTQIAQLGRASKVVVTKENTTIVEGAGETDKISARVTQIRAQVEETTSEFDR EKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDALNSTRAAVEEGIVSGGGTALVNV YNKVAAVEAEGDAQTGINIVLRALEEPIRQIAHNAGLEGSVIVERLKNEEIGVGFNAATG EWVNMIEKGIVDPTKVTRSALQNAASVAAMFLTTEAVVADKPEENGGGAGMPDMGGMGGM GGMM

CH60_BACSU

P28598

1617

4.2854

57572.0

538

GspA

584

513

5.05

39513

13630

858

5.089

33368.4

286

P25148

286

gspA

F:transferase activity, transferring glycosyl... [GO:0016757]
P:response to stress [GO:0006950]

5.1076

33521.9

1423

Bacillus subtilis

GspA

General stress protein A

GspA

5 references

MRKDEIMHIVSCADDNYARHLGGMFVSLLTNMDQEREVKLYVIDGGIKPDNKKRLEETTL KFGVPIEFLEVDTNMYEHAVESSHITKAAYYRISIPDLIKDESIKRMIYIDCDALVLEDI SKLWDLDIAPYTVAAVEDAGQHERLKEMNVTDTGKYFNSGIMIIDFESWRKQNITEKVIN FINEHPDEDFLVLHDQDALNAILYDQWYELHPRWNAQTYIMLKLKTPSTLLGRKQYNETR ENPAIVHFCGGEKPWNSNTKHPYRDEYFHYMSYTKWNTIGNPAINQ

GSPA_BACSU

P25148

0.0

GspA

551

512

5.16

39653

13629

858

5.089

33368.4

286

P25148

286

gspA

F:transferase activity, transferring glycosyl... [GO:0016757]
P:response to stress [GO:0006950]

5.1076

33521.9

1423

Bacillus subtilis

GspA

General stress protein A

GspA

5 references

GSPA_BACSU

P25148

0.0

GtaB

612

514

4.96

39402

13627

876

4.913

32917.4

292

glucosylation of teichoic acid

Q05852

292

Catalyzes the formation of UDP-glucose from glucose-1-phosphate and UTP. This is an intermediate step in the biosynthesis of diglucosyl-diacylglycerol (Glc2-DAG), i.e. the predominant glycolipid found in B.subtilis membrane, which is also used as a membrane anchor for lipoteichoic acid (LTA). Has a role in the biosynthesis of all phosphate-containing envelope polymers, since UDP-glucose serves as a glucosyl donor not only for the biosynthesis of LTA but also for wall teichoic acids (WTAs). Is required for biofilm formation. This is likely due to another role of UDP-glucose, which might also act as a metabolic signal regulating biofilm formation or may be involved in some unknown biosynthetic pathway essential for biofilm formation, e.g. the synthesis of an exopolysaccharide.

gtaB

F:UTP:glucose-1-phosphate uridylyltransferase... [GO:0003983]
P:biosynthetic process [GO:0009058]
P:response to stress [GO:0006950]
P:UDP-glucose metabolic process [GO:0006011]

4.8218

33069.93

1423

Bacillus subtilis

GtaB

UTP--glucose-1-phosphate uridylyltransferase

GtaB

6 references

MKKVRKAIIPAAGLGTRFLPATKAMPKEMLPIVDKPTIQYIIEEAVEAGIEDIIIVTGKS KRAIEDHFDYSPELERNLEEKGKTELLEKVKKASNLADIHYIRQKEPKGLGHAVWCARNF IGDEPFAVLLGDDIVQAETPGLRQLMDEYEKTLSSIIGVQQVPEEETHRYGIIDPLTSEG RRYQVKNFVEKPPKGTAPSNLAILGRYVFTPEIFMYLEEQQVGAGGEIQLTDAIQKLNEI QRVFAYDFEGKRYDVGEKLGFITTTLEFAMQDKELRDQLVPFMEGLLNKEEI

GTAB_BACSU

Q05852

867

5.1766

32451.1

288

Hag

662

420

4.81

50346

13751

912

4.782

32472.0

304

P02968

304

Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.

hag

C:bacterial-type flagellum filament [GO:0009420]
C:cell wall [GO:0005618]
C:extracellular region [GO:0005576]
F:structural molecule activity [GO:0005198]
P:ciliary or flagellar motility [GO:0001539]

4.7354

32626.22

1423

Bacillus subtilis

Hag

Flagellin

Hag

9 references

MRINHNIAALNTLNRLSSNNSASQKNMEKLSSGLRINRAGDDAAGLAISEKMRGQIRGLE MASKNSQDGISLIQTAEGALTETHAILQRVRELVVQAGNTGTQDKATDLQSIQDEISALT DEIDGISNRTEFNGKKLLDGTYKVDTATPANQKNLVFQIGANATQQISVNIEDMGADALG IKEADGSIAALHSVNDLDVTKFADNAADTADIGFDAQLKVVDEAINQVSSQRAKLGAVQN RLEHTINNLSASGENLTAAESRIRDVDMAKEMSEFTKNNILSQASQAMLAQANQQPQNVL QLLR

FLA_BACSU

P02968

0.0

Icd

664

358

4.81

58976

13729

1269

4.833

46255.0

423

P39126

423

icd

F:isocitrate dehydrogenase (NADP+) activity [GO:0004450]
F:magnesium ion binding [GO:0000287]
F:NAD or NADH binding [GO:0051287]
P:glyoxylate cycle [GO:0006097]
P:oxidation reduction [GO:0055114]
P:tricarboxylic acid cycle [GO:0006099]

4.7445

46417.64

1423

Bacillus subtilis

Icd

Isocitrate dehydrogenase [NADP]

Icd

5 references

MAQGEKITVSNGVLNVPNNPIIPFIEGDGTGPDIWNAASKVLEAAVEKAYKGEKKITWKE VYAGEKAYNKTGEWLPAETLDVIREYFIAIKGPLTTPVGGGIRSLNVALRQELDLFVCLR PVRYFTGVPSPVKRPEDTDMVIFRENTEDIYAGIEYAKGSEEVQKLISFLQNELNVNKIR FPETSGIGIKPVSEEGTSRLVRAAIDYAIEHGRKSVTLVHKGNIMKFTEGAFKNWGYELA EKEYGDKVFTWAQYDRIAEEQGKDAANKAQSEAEAAGKIIIKDSIADIFLQQILTRPNEF DVVATMNLNGDYISDALAAQVGGIGIAPGANINYETGHAIFEATHGTAPKYAGLDKVNPS SVILSGVLLLEHLGWNEAADLVIKSMEKTIASKVVTYDFARLMDGATEVKCSEFGEELIK NMD

IDH_BACSU

P39126

0.0

IlvC

433

407

5.56

52047

13760

1026

5.37

37302.2

342

P37253

342

ilvC

F:coenzyme binding [GO:0050662]
F:ketol-acid reductoisomerase activity [GO:0004455]
P:branched chain family amino acid biosynthet... [GO:0009082]
P:oxidation reduction [GO:0055114]

5.4597

37457.57

1423

Bacillus subtilis

IlvC

Ketol-acid reductoisomerase

IlvC

4 references

MVKVYYNGDIKENVLAGKTVAVIGYGSQGHAHALNLKESGVDVIVGVRQGKSFTQAQEDG HKVFSVKEAAAQAEIIMVLLPDEQQQKVYEAEIKDELTAGKSLVFAHGFNVHFHQIVPPA DVDVFLVAPKGPGHLVRRTYEQGAGVPALFAIYQDVTGEARDKALAYAKGIGGARAGVLE TTFKEETETDLFGEQAVLCGGLSALVKAGFETLTEAGYQPELAYFECLHELKLIVDLMYE EGLAGMRYSISDTAQWGDFVSGPRVVDAKVKESMKEVLKDIQNGTFAKEWIVENQVNRPR FNAINASENEHQIEVVGRKLREMMPFVKQGKKKEAVVSVAQN

ILVC_BACSU

P37253

1005

4.9518

37013.8

334

KatA

203

259

6.34

76501

13035

1449

6.151

54566.7

483

P26901

483

Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.

katA

C:cytoplasm [GO:0005737]
F:catalase activity [GO:0004096]
F:heme binding [GO:0020037]
P:hydrogen peroxide catabolic process [GO:0042744]
P:oxidation reduction [GO:0055114]

6.5182

54791.13

1423

Bacillus subtilis

KatA

Vegetative catalase

KatA

7 references

MSSNKLTTSWGAPVGDNQNSMTAGSRGPTLIQDVHLLEKLAHFNRERVPERVVHAKGAGA HGYFEVTNDVTKYTKAAFLSEVGKRTPLFIRFSTVAGELGSADTVRDPRGFAVKFYTEEG NYDIVGNNTPVFFIRDAIKFPDFIHTQKRDPKTHLKNPTAVWDFWSLSPESLHQVTILMS DRGIPATLRHMHGFGSHTFKWTNAEGEGVWIKYHFKTEQGVKNLDVNTAAKIAGENPDYH TEDLFNAIENGDYPAWKLYVQIMPLEDANTYRFDPFDVTKVWSQKDYPLIEVGRMVLDRN PENYFAEVEQATFSPGTLVPGIDVSPDKMLQGRLFAYHDAHRYRVGANHQALPINRARNK VNNYQRDGQMRFDDNGGGSVYYEPNSFGGPKESPEDKQAAYPVQGIADSVSYDHYDHYTQ AGDLYRLMSEDERTRLVENIVNAMKPVEKEEIKLRQIEHFYKADPEYGKRVAEGLGLPIK KDS

CATA_BACSU

P26901

1524

5.1325

58612.0

507

Mdh

691

446

4.71

47065

13196

936

4.727

33489.7

312

P49814

312

Catalyzes the reversible oxidation of malate to oxaloacetate (By similarity).

mdh

F:binding [GO:0005488]
F:L-malate dehydrogenase activity [GO:0030060]
P:glycolysis [GO:0006096]
P:malate metabolic process [GO:0006108]
P:oxidation reduction [GO:0055114]
P:tricarboxylic acid cycle [GO:0006099]

4.644

33643.43

1423

Bacillus subtilis

Mdh

Malate dehydrogenase

Mdh

6 references

MGNTRKKVSVIGAGFTGATTAFLIAQKELADVVLVDIPQLENPTKGKALDMLEASPVQGF DAKITGTSNYEDTAGSDIVVITAGIARKPGMSRDDLVSTNEKIMRSVTQEIVKYSPDSII VVLTNPVDAMTYAVYKESGFPKERVIGQSGVLDTARFRTFVAEELNLSVKDVTGFVLGGH GDDMVPLVRYSYAGGIPLETLIPKERIDAIVERTRKGGGEIVNLLGNGSAYYAPAASLTE MVEAILKDQRRVLPTIAYLEGEYGYEGIYLGVPTIVGGNGLEQIIELELTDYERAQLNKS VESVKNVMKVLS

MDH_BACSU

P49814

0.0

Pgk

674

348

4.78

60512

13723

1182

4.768

42030.1

394

P40924

394

pgk

C:cytoplasm [GO:0005737]
F:ATP binding [GO:0005524]
F:phosphoglycerate kinase activity [GO:0004618]
P:glycolysis [GO:0006096]

4.7055

42190.17

1423

Bacillus subtilis

Pgk

Phosphoglycerate kinase

Pgk

4 references

MNKKTLKDIDVKGKVVFCRVDFNVPMKDGEVTDDTRIRAALPTIKHLADQGAKVLLASHL GRPKGEVVEELRLTPVAARLGELLGKEVKKADEAYGDAVKAQISEMKDGDVLVLENVRFY PGEEKNDPELAKAFAELADVYVNDAFGAAHRAHASTAGIAEHLPAVAGFLMEKELDVLGK AVSNPDRPFTAIIGGAKVKDKIGVIESLLDKVDNLIIGGGLAYTFVKALGYEVGKSLLEE DKIELAKSFMDRAKEKGVNFYMPEDVLVADDFSNDANVKIVPISEIPSDLEAIDIGTKTR ETYADVIKNSKLVVWNGPMGVFEIDLFAQGTKAVAEALAEAKDTYSVIGGGDSAAAVEKF GLADKMSHISTGGGASLEFMEGKELPGVAALNDK

PGK_BACSU

P40924

1191

4.9614

42601.6

396

PtsH

676

997

4.68

3585

13610

264

4.584

9051.3

transfers phosphate from enzyme I to specific enzymes II/III permeases; mediates carbon catabolite repression (CCR)

P08877

General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the permease (enzymes II/III).

ptsH

C:cytoplasm [GO:0005737]
F:kinase activity [GO:0016301]
F:sugar:hydrogen symporter activity [GO:0005351]
P:phosphoenolpyruvate-dependent sugar phospho... [GO:0009401]
P:regulation of transcription [GO:0045449]
P:transcription [GO:0006350]

4.5185

9189.33

1423

Bacillus subtilis

PtsH

Phosphocarrier protein HPr

PtsH

13 references

MAQKTFKVTADSGIHARPATVLVQTASKYDADVNLEYNGKTVNLKSIMGVMSLGIAKGAE ITISASGADENDALNALEETMKSEGLGE

PTHP_BACSU

P08877

267

4.2677

9495.7

RsbW

870

775

4.08

17194

13432

480

4.285

17849.6

160

negative regulation of sigma-B-dependent gene expression; phosphorylation of RsbV

P17904

160

Negative regulator of sigma-B activity. Phosphorylates and inactivates its specific antagonist protein, rsbV. Upon phosphorylation of rsbV, rsbW is released and binds to sigma-B, thereby blocking its ability to form an RNA polymerase holoenzyme (E-sigma-B).

rsbW

F:ATP binding [GO:0005524]
F:protein serine/threonine kinase activity [GO:0004674]
F:sigma factor antagonist activity [GO:0016989]
P:negative regulation of transcription, DNA-d... [GO:0045892]
P:protein phosphorylation [GO:0006468]
P:response to stress [GO:0006950]

4.231

17992.95

1423

Bacillus subtilis

RsbW

Serine-protein kinase rsbW

RsbW

9 references

MKNNADYIEMKVPAQPEYVGIIRLTLSGVASRMGYTYDEIEDLKIAVSEACTNAVQHAYK EDKNGEVSIRFGVFEDRLEVIVADEGDSFDFDQKQQDLGPYTPSHTVDQLSEGGLGLYLM ETLMDEVRVQNHSGVTVAMTKYLNGERVDHDTTIKNYETN

RSBW_BACSU

P17904

480

4.4501

17921.2

159

SodA

608

665

4.95

25484

13575

606

5.203

22428.8

202

P54375

202

Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

sodA

C:cytoplasm [GO:0005737]
F:metal ion binding [GO:0046872]
F:superoxide dismutase activity [GO:0004784]
P:oxidation reduction [GO:0055114]
P:response to stress [GO:0006950]
P:superoxide metabolic process [GO:0006801]

5.0627

22489.88

1423

Bacillus subtilis

SodA

Superoxide dismutase [Mn]

SodA

8 references

MAYELPELPYAYDALEPHIDKETMTIHHTKHHNTYVTNLNKAVEGNTALANKSVEELVAD LDSVPENIRTAVRNNGGGHANHKLFWTLLSPNGGGEPTGALAEEINSVFGSFDKFKEQFA AAAAGRFGSGWAWLVVNNGKLEITSTPNQDSPLSEGKTPILGLDVWEHAYYLNYQNRRPD YISAFWNVVNWDEVARLYSEAK

SODM_BACSU

P54375

600

4.8565

22711.3

199

Spot_01

149

320

6.51

65138

13091

Spot_02

153

461

6.48

45263

13222

YdbD

644

513

4.86

39485

13628

819

4.858

30105.8

273

unknown

D4G5B9

273

ydbD

F:oxidoreductase activity [GO:0016491]
F:transition metal ion binding [GO:0046914]
P:oxidation reduction [GO:0055114]

4.7875

30316.31

645657

Bacillus subtilis subsp. natto BEST195

YdbD

1 references

MFKHTKMLQHPAKPDRPDPLFAKKMQEILGGQFGEISVAMQYLFQGWNTRGNEKYKDLLM DTATEELGHVEMIATMIARLLEDAPLDQQEKAAEDPVIGSILGGMNPHHAIVSGLGAMPE SSTGVPWSGGYIVASGNLLADFRANLNAESQGRLQVARLFEMTDDKGVKDMLSFLLARDT MHQNQWLAAIKELEAQEGPVVPGTFPKALEKQEFSHQLINFSEGEESAQQNWLNEKAPDG EAFEYVKEAKTFGEKPELKPTPPFVHNTLPGRE

D4G5B9_BACNA

D4G5B9

0.0

YtxH

565

743

5.08

19457

13588

456

5.107

16542.7

152

unknown

P40780

151

ytxH

5.0722

Complete proteome

16554.55

1423

Bacillus subtilis

YtxH

Uncharacterized protein ytxH

YtxH

3 references

MSKDGINSKDFLIGTLIGGIIGATTALFLAPKSGKELRDDLGSQAVALRDKTDKMTADAK EKGTQYVSIAKDKTSNITQLVADQSGQIMNKVKDLRDRSKSDKTDSSTAMQDMREEAMQA ADETKDQVLQTKEDVKDELKDAQKQAEQLNR

YTXH_BACSU

P40780

0.0

YvyD

518

622

5.25

29100

13563

567

5.184

21833.7

189

unknown

P28368

189

yvyD

F:binding [GO:0005488]
P:primary metabolic process [GO:0044238]

5.1806

Complete proteome

21979.65

1423

Bacillus subtilis

YvyD

Uncharacterized protein yvyD

YvyD

4 references

MNYNIRGENIEVTPALKDHVERKIGKLERYFDHSVDADVNVNLKFYNDKESKVEVTIPMT DLALRSEVHNEDMYNAIDLATNKLERQIRKHKTKVNRKFREQGSPKYLLANGLGSDTDIA VQDDIEEEESLDIVRQKRFNLKPMDSEEAILQMNMLGHNFFVFTNAETNLTNVVYRRNDG KYGLIEPTE

YVYD_BACSU

P28368

0.0

Delta2D Labelsfor Project 'Demonstration'

Labels

Delta2D Labels
for Project 'Demonstration'