Delta2D Report: Labels
for Project 'Demonstration'

Project Properties

Author DECODON Project Creation Date Wed Feb 22 20:00:00 CET 2006
Use Internal Standard no Pool C:\data\demopool
Description Delta2D demonstration project. A time-course experiment with three samples. We thank Falko Hochgräfe for the gel images
Report created by user "bielz" with Delta2D, Fri Jul 15 11:46:13 CEST 2016. Please let us know if you have any comment or suggestion using our contact form.

Labels

Table shows label data for the expression profile of selected spots on gel image 'control_01'.
Total number of selected spots shown in this report: 9.

control_01 control Fused Images
  control_01 Fused Image
Spot Label name(s) Pi/MW Estimation GenoList Uniprot Label name(s) Pi/MW Estimation GenoList
ID Name Pi MW Gene Size (bp) 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 Name Pi MW Gene Size (bp) Protein Size (aa) Function
(no label) N.A. N.A. (no label) N.A. N.A.
(no label) N.A. N.A. (no label) N.A. N.A.
EF-Ts N.A. N.A.
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 (By similarity).
tsf
4.9005
32353.77
224308
Bacillus subtilis (strain 168)
EF-Ts
Elongation factor Ts
EF-Ts
MAITAQQVKELREKTGAGMMDCKKALTETDGDMDKAIDLLREKGIAKAAKKADRIAAEGS TLIKTDGNKGVILEVNSETDFVAKNEGFKELLNTLADHLLANTPADVEEAMGQKMENGST VEEYITSAVAKIGEKITLRRFTVLTKDDSSAFGAYLHMGGRIGVLTVLNGTTDEETAKDI AMHVAAVNPRYISRDQVSEEETNHERQILTQQALQEGKPENIVAKMVEGRLNKFFEEICL LDQAFVKNPDEKVKQVIAAKNATVQTFVRYEVGEGIEKRQENFAEEVMNQVKK
EFTS_BACSU
EF-Ts N.A. N.A.
0
0
(no label) N.A. N.A. (no label) N.A. N.A.
(no label) N.A. N.A. (no label) N.A. N.A.
(no label) N.A. N.A. (no label) N.A. N.A.
EF-G N.A. N.A.
0
0
P80868
692
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity).
fusA
4.5136
76616.6
224308
Bacillus subtilis (strain 168)
EF-G
Elongation factor G
EF-G
MAREFSLEKTRNIGIMAHIDAGKTTTTERILFYTGRIHKIGETHEGASQMDWMEQEQERG ITITSAATTAQWKGYRVNIIDTPGHVDFTVEVERSLRVLDGAVAVLDAQSGVEPQTETVW RQATTYGVPRIVFVNKMDKIGADFLYSVGTLRDRLQANAHAIQLPIGAEDNFEGIIDLVE NVAYFYEDDLGTRSDAKEIPEEYKEQAEELRNSLIEAVCELDEELMDKYLEGEEITIDEL KAGIRKGTLNVEFYPVLVGSAFKNKGVQLVLDAVLDYLPAPTDVAAIKGTRPDTNEEIER HSSDEEPFSALAFKVMTDPYVGKLTFFRVYSGTLDSGSYVKNSTKGKRERVGRILQMHAN SREEISTVYAGDIAAAVGLKDTTTGDTLCDEKDLVILESMEFPEPVIDVAIEPKSKADQD KMGIALAKLAEEDPTFRTQTNPETGQTIISGMGELHLDIIVDRMKREFKVEANVGAPQVA YRETFRTGAKVEGKFVRQSGGRGQFGHVWIEFEPNEEGAGFEFENAIVGGVVPREYIPAV QAGLEDALENGVLAGFPLIDIKAKLFDGSYHDVDSNEMAFKVAASMALKNAVSKCNPVLL EPIMKVEVVIPEEYMGDIMGDITSRRGRVEGMEARGNAQVVRAMVPLAEMFGYATALRSN TQGRGTFTMHMDHYEEVPKSVAEEIIKKNKGE
EFG_BACSU
EF-G N.A. N.A.
0
0
(no label) N.A. N.A. (no label) N.A. N.A.
(no label) N.A. N.A. (no label) N.A. N.A.

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.
Total number of labels shown in this report: 29.

Label Spot Pi/MW Estimation GenoList Uniprot
Name X Y ID Pi MW Gene Size (bp) 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
AhpC 876 689
N.A. N.A.
561
187
P80239
187
Directly reduces organic hydroperoxides in its reduced dithiol form.
ahpC
4.2224
20627.12
224308
Bacillus subtilis (strain 168)
AhpC
Alkyl hydroperoxide reductase subunit C
AhpC
MSLIGKEVLPFEAKAFKNGEFIDVTNEDLKGQWSVFCFYPADFSFVCPTELEDLQEQYAA LKELGVEVYSVSTDTHFVHKGWHDSSEKISKITYAMIGDPSQTISRNFDVLDEETGLADR GTFIIDPDGVIQTVEINAGGIGRDASNLVNKVKAAQYVRQNPGEVCPAKWEEGGETLTPS LDLVGKI
AHPC_BACSU
AhpF 711 271
N.A. N.A.
1527
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
4.6273
54874.4
224308
Bacillus subtilis (strain 168)
AhpF
NADH dehydrogenase
AhpF
MVLDANIKAQLNQYMQLIENDIVLKVSAGEDDTSKDMLALVDELASMSSKISVEKAELNR TPSFSVNRVGEDTGVTFAGIPLGHEFTSLVLALLQVSGRPPKVDQKVIDQVKKISGEYHF ESYISLTCHNCPDVVQALNMMSVLNPNITHTMIDGAAYKAEVESKNIMAVPTVYLNGESF GSGRMTLEEILAKMGSGTDASEFADKEPFDVLVVGGGPAGASAAIYTARKGIRTGVVAER FGGQVLDTMSIENFISVKATEGPKLAASLEEHVKEYDIDVMNLQRAKRLEKKDLFELELE NGAVLKSKTVILSTGARWRNVNVPGEQEFKNKGVAYCPHCDGPLFEGKDVAVIGGGNSGI EAAIDLAGIVNHVTVLEFAPELKADEVLQKRLYSLPNVTVVKNAQTKEITGDQSVNGITY VDRETGEEKHVELQGVFVQIGLVPNTEWLEGTVERNRMGEIIVDKHGATSVPGLFAAGDC TDSAYNQIIISMGSGATAALGAFDYLIRN
DHNA_BACSU
AroA 450 398
N.A. N.A.
1074
358
P39912
358
aroA
5.3532
39539.46
224308
Bacillus subtilis (strain 168)
AroA
Protein AroA(G)
AroA
MSNTELELLRQKADELNLQILKLINERGNVVKEIGKAKEAQGVNRFDPVRERTMLNNIIE NNDGPFENSTIQHIFKEIFKAGLELQEEDHSKALLVSRKKKPEDTIVDIKGEKIGDGQQR FIVGPCAVESYEQVAEVAAAAKKQGIKILRGGAFKPRTSPYDFQGLGVEGLQILKRVADE FDLAVISEIVTPAHIEEALDYIDVIQIGARNMQNFELLKAAGAVKKPVLLKRGLAATISE FINAAEYIMSQGNDQIILCERGIRTYETATRNTLDISAVPILKQETHLPVFVDVTHSTGR RDLLLPTAKAALAIGADGVMAEVHPDPSVALSDSAQQMAIPEFEKWLNELKPMVKVNA
AROG_BACSU
CysK 384 535
N.A. N.A.
924
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
5.5093
32819.6
224308
Bacillus subtilis (strain 168)
CysK
Cysteine synthase
CysK
MVRVANSITELIGNTPIVKLNRLADENSADVYLKLEYMNPGSSVKDRIGLAMIEAAEKEG KLKAGNTIIEPTSGNTGIGLAMVAAAKGLKAILVMPDTMSMERRNLLRAYGAELVLTPGA EGMKGAIKKAEELAEKHGYFVPQQFNNPSNPEIHRQTTGKEIVEQFGDDQLDAFVAGIGT GGTITGAGEVLKEAYPSIKIYAVEPSDSPVLSGGKPGPHKIQGIGAGFVPDILNTEVYDE IFPVKNEEAFEYARRAAREEGILGGISSGAAIYAALQVAKKLGKGKKVLAIIPSNGERYL STPLYQFD
CYSK_BACSU
DnaK 751 178
N.A. N.A.
1833
611
P17820
611
Acts as a chaperone.
dnaK
4.4949
66002.12
224308
Bacillus subtilis (strain 168)
DnaK
Chaperone protein DnaK
DnaK
MSKVIGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAFKNGERQVGEVAKRQSITN PNTIMSIKRHMGTDYKVEIEGKDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYF NDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDKTDEDQTILVYDLGGGTFDVSILE LGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVSEFKKENGIDLSKDKMALQRLKDAAEKAK KDLSGVSSTQISLPFITAGEAGPLHLELTLTRAKFEELSSHLVERTMGPVRQALQDAGLS ASEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAIQGGVITGDVKDVV LLDVTPLSLGIETMGGVFTKLIDRNTTIPTSKSQVFSTAADNQTAVDIHVLQGERPMSAD NKTLGRFQLTDIPPAPRGVPQIEVSFDIDKNGIVNVRAKDLGTGKEQNITIKSSSGLSDE EIERMVKEAEENADADAKKKEEIEVRNEADQLVFQTEKTLKDLEGKVDEEQVKKANDAKD ALKAAIEKNEFEEIKAKKDELQTIVQELSMKLYEEAAKAQQAQGGANAEGKADDNVVDAE YEEVNDDQNKK
DNAK_BACSU
Dps 778 804
N.A. N.A.
435
145
P80879
145
dps
4.368
16593.73
224308
Bacillus subtilis (strain 168)
Dps
General stress protein 20U
Dps
MSEQLIQAVNKQVANWTVMYVKLHNYHWYVKGKDFFTLHEKFEELYNETATYIDDLAERL LALNGKPIATMKESLETASVKEAAGNETAEQMVQSVYDDFTVIAEELKNGMDLADEVGDE TTGDMLLAIHQNIEKHNWMLKAYLG
G20U_BACSU
Dps 815 783
N.A. N.A.
435
145
P80879
145
dps
4.368
16593.73
224308
Bacillus subtilis (strain 168)
Dps
General stress protein 20U
Dps
MSEQLIQAVNKQVANWTVMYVKLHNYHWYVKGKDFFTLHEKFEELYNETATYIDDLAERL LALNGKPIATMKESLETASVKEAAGNETAEQMVQSVYDDFTVIAEELKNGMDLADEVGDE TTGDMLLAIHQNIEKHNWMLKAYLG
G20U_BACSU
EF-G 708 131
N.A. N.A.
0
0
P80868
692
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity).
fusA
4.5136
76616.6
224308
Bacillus subtilis (strain 168)
EF-G
Elongation factor G
EF-G
MAREFSLEKTRNIGIMAHIDAGKTTTTERILFYTGRIHKIGETHEGASQMDWMEQEQERG ITITSAATTAQWKGYRVNIIDTPGHVDFTVEVERSLRVLDGAVAVLDAQSGVEPQTETVW RQATTYGVPRIVFVNKMDKIGADFLYSVGTLRDRLQANAHAIQLPIGAEDNFEGIIDLVE NVAYFYEDDLGTRSDAKEIPEEYKEQAEELRNSLIEAVCELDEELMDKYLEGEEITIDEL KAGIRKGTLNVEFYPVLVGSAFKNKGVQLVLDAVLDYLPAPTDVAAIKGTRPDTNEEIER HSSDEEPFSALAFKVMTDPYVGKLTFFRVYSGTLDSGSYVKNSTKGKRERVGRILQMHAN SREEISTVYAGDIAAAVGLKDTTTGDTLCDEKDLVILESMEFPEPVIDVAIEPKSKADQD KMGIALAKLAEEDPTFRTQTNPETGQTIISGMGELHLDIIVDRMKREFKVEANVGAPQVA YRETFRTGAKVEGKFVRQSGGRGQFGHVWIEFEPNEEGAGFEFENAIVGGVVPREYIPAV QAGLEDALENGVLAGFPLIDIKAKLFDGSYHDVDSNEMAFKVAASMALKNAVSKCNPVLL EPIMKVEVVIPEEYMGDIMGDITSRRGRVEGMEARGNAQVVRAMVPLAEMFGYATALRSN TQGRGTFTMHMDHYEEVPKSVAEEIIKKNKGE
EFG_BACSU
EF-Ts 589 467
N.A. N.A.
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 (By similarity).
tsf
4.9005
32353.77
224308
Bacillus subtilis (strain 168)
EF-Ts
Elongation factor Ts
EF-Ts
MAITAQQVKELREKTGAGMMDCKKALTETDGDMDKAIDLLREKGIAKAAKKADRIAAEGS TLIKTDGNKGVILEVNSETDFVAKNEGFKELLNTLADHLLANTPADVEEAMGQKMENGST VEEYITSAVAKIGEKITLRRFTVLTKDDSSAFGAYLHMGGRIGVLTVLNGTTDEETAKDI AMHVAAVNPRYISRDQVSEEETNHERQILTQQALQEGKPENIVAKMVEGRLNKFFEEICL LDQAFVKNPDEKVKQVIAAKNATVQTFVRYEVGEGIEKRQENFAEEVMNQVKK
EFTS_BACSU
EF-Tu 680 317
N.A. N.A.
0
0
P33166
396
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
tuf
4.6467
43593.27
224308
Bacillus subtilis (strain 168)
EF-Tu
Elongation factor Tu
EF-Tu
MAKEKFDRSKSHANIGTIGHVDHGKTTLTAAITTVLHKKSGKGTAMAYDQIDGAPEERER GITISTAHVEYETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREH ILLSKNVGVPYIVVFLNKCDMVDDEELLELVEMEVRDLLSEYDFPGDDVPVVKGSALKAL EGDAEWEAKIFELMDAVDEYIPTPERDTEKPFMMPVEDVFSITGRGTVATGRVERGQVKV GDEVEIIGLQEENKKTTVTGVEMFRKLLDYAEAGDNIGALLRGVSREEIQRGQVLAKPGT ITPHSKFKAEVYVLSKEEGGRHTPFFSNYRPQFYFRTTDVTGIIHLPEGVEMVMPGDNTE MNVELISTIAIEEGTRFSIREGGRTVGSGVVSTITE
EFTU_BACSU
Eno 772 340
N.A. N.A.
1290
430
P37869
430
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
eno
4.4037
46581.39
224308
Bacillus subtilis (strain 168)
Eno
Enolase
Eno
MPYIVDVYAREVLDSRGNPTVEVEVYTETGAFGRALVPSGASTGEYEAVELRDGDKDRYL GKGVLTAVNNVNEIIAPELLGFDVTEQNAIDQLLIELDGTENKGKLGANAILGVSMACAR AAADFLQIPLYQYLGGFNSKTLPVPMMNIVNGGEHADNNVDIQEFMIMPVGAPNFREALR MGAQIFHSLKSVLSAKGLNTAVGDEGGFAPNLGSNEEALQTIVEAIEKAGFKPGEEVKLA MDAASSEFYNKEDGKYHLSGEGVVKTSAEMVDWYEELVSKYPIISIEDGLDENDWEGHKL LTERLGKKVQLVGDDLFVTNTKKLSEGIKNGVGNSILIKVNQIGTLTETFDAIEMAKRAG YTAVISHRSGETEDSTIADIAVATNAGQIKTGAPSRTDRVAKYNQLLRIEDQLAETAQYH GINSFYNLNK
ENO_BACSU
GapA 544 371
N.A. N.A.
1005
335
catabolic enzyme
E0U2V1
340
cggR
5.8363
37410.17
655816
Bacillus subtilis subsp. spizizenii (strain ATCC 23059 / NRRL B-14472 / W23)
GapA
GapA
MNQLIQAQKKLLPDLLLVMQKRFEILQYIRLTEPIGRRSLSASLGISERVLRGEVQFLKE QNLVDIKTNGMTLTEEGYELLSVLEDTMKDVLGLTLLEKTLKERLNLKDAIIVSGDSDQS PWVKKEMGRAAVACMKKRFSGKNIVAVTGGTTIEAVAEMMTPDSKNRELLFVPARGGLGE DVKNQANTICAHMAEKASGTYRLLFVPGQLSQGAYSSIIEEPSVKEVLNTIKSASMLVHG IGEAKTMAQRRNTPLEDLKKIDDNDAVTEAFGYYFNVDGEVVHKVHSVGMQLDDIDAIPD IIAVAGGSSKAEAIEAYFKKPRNTVLVTDEGAAKKLLRDE
E0U2V1_BACPZ
GlnA 629 297
N.A. N.A.
1332
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
5.4998
406812.3
224308
Bacillus subtilis (strain 168)
GlnA
Plipastatin synthase subunit D
GlnA
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
GroEL 748 213
N.A. N.A.
1632
544
P28598
544
Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
groL
4.4284
57424.58
224308
Bacillus subtilis (strain 168)
GroEL
60 kDa chaperonin
GroEL
MAKEIKFSEEARRAMLRGVDALADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIE LEDAFENMGAKLVAEVASKTNDVAGDGTTTATVLAQAMIREGLKNVTAGANPVGVRKGME QAVAVAIENLKEISKPIEGKESIAQVAAISAADEEVGSLIAEAMERVGNDGVITIEESKG FTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDNPYILITDKKITNIQEILPVLEQVVQ QGKPLLLIAEDVEGEALATLVVNKLRGTFNAVAVKAPGFGDRRKAMLEDIAVLTGGEVIT EDLGLDLKSTQIAQLGRASKVVVTKENTTIVEGAGETDKISARVTQIRAQVEETTSEFDR EKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDALNSTRAAVEEGIVSGGGTALVNV YNKVAAVEAEGDAQTGINIVLRALEEPIRQIAHNAGLEGSVIVERLKNEEIGVGFNAATG EWVNMIEKGIVDPTKVTRSALQNAASVAAMFLTTEAVVADKPEENGGGAGMPDMGGMGGM GGMM
CH60_BACSU
GspA 584 513
N.A. N.A.
858
286
P25148
286
gspA
  • F:transferase activity, transferring glycosyl groups [GO:0016757]
  • P:polysaccharide biosynthetic process [GO:0000271]
5.1072
33521.99
224308
Bacillus subtilis (strain 168)
GspA
General stress protein A
GspA
MRKDEIMHIVSCADDNYARHLGGMFVSLLTNMDQEREVKLYVIDGGIKPDNKKRLEETTL KFGVPIEFLEVDTNMYEHAVESSHITKAAYYRISIPDLIKDESIKRMIYIDCDALVLEDI SKLWDLDIAPYTVAAVEDAGQHERLKEMNVTDTGKYFNSGIMIIDFESWRKQNITEKVIN FINEHPDEDFLVLHDQDALNAILYDQWYELHPRWNAQTYIMLKLKTPSTLLGRKQYNETR ENPAIVHFCGGEKPWNSNTKHPYRDEYFHYMSYTKWNTIGNPAINQ
GSPA_BACSU
GspA 551 512
N.A. N.A.
858
286
P25148
286
gspA
  • F:transferase activity, transferring glycosyl groups [GO:0016757]
  • P:polysaccharide biosynthetic process [GO:0000271]
5.1072
33521.99
224308
Bacillus subtilis (strain 168)
GspA
General stress protein A
GspA
MRKDEIMHIVSCADDNYARHLGGMFVSLLTNMDQEREVKLYVIDGGIKPDNKKRLEETTL KFGVPIEFLEVDTNMYEHAVESSHITKAAYYRISIPDLIKDESIKRMIYIDCDALVLEDI SKLWDLDIAPYTVAAVEDAGQHERLKEMNVTDTGKYFNSGIMIIDFESWRKQNITEKVIN FINEHPDEDFLVLHDQDALNAILYDQWYELHPRWNAQTYIMLKLKTPSTLLGRKQYNETR ENPAIVHFCGGEKPWNSNTKHPYRDEYFHYMSYTKWNTIGNPAINQ
GSPA_BACSU
GtaB 612 514
N.A. N.A.
876
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 activity [GO:0003983]
  • P:enterobacterial common antigen biosynthetic process [GO:0009246]
  • P:UDP-glucose metabolic process [GO:0006011]
4.8217
33070.03
224308
Bacillus subtilis (strain 168)
GtaB
UTP--glucose-1-phosphate uridylyltransferase
GtaB
MKKVRKAIIPAAGLGTRFLPATKAMPKEMLPIVDKPTIQYIIEEAVEAGIEDIIIVTGKS KRAIEDHFDYSPELERNLEEKGKTELLEKVKKASNLADIHYIRQKEPKGLGHAVWCARNF IGDEPFAVLLGDDIVQAETPGLRQLMDEYEKTLSSIIGVQQVPEEETHRYGIIDPLTSEG RRYQVKNFVEKPPKGTAPSNLAILGRYVFTPEIFMYLEEQQVGAGGEIQLTDAIQKLNEI QRVFAYDFEGKRYDVGEKLGFITTTLEFAMQDKELRDQLVPFMEGLLNKEEI
GTAB_BACSU
Hag 662 420
N.A. N.A.
912
304
A0A0K6MGG5
462
BN2127_JRS10_00642
    8.5596
      50607.65
      1423
      Bacillus subtilis
      Hag
      Hag
      MKKKSSKQKRKCPPFYLPMYGINNWCSIRAAALEELEEQEAAPKNKARPKYVSLQNAVMS RIIDNQITKRQQKNKPLSTHTEQIVPSEQAEKKTEENIPVAINKKAESEIPAAIINQVKK IKEALATSGDRQTEKTIIIHPPTPEISKVKKGGRYVHAEGLHSHAEGTASHAEGLLTHAK GSFSHAEGSKTKATGHSSHSEGSETTAGGSYSHAEGKHTIALGEAAHAEGTATIANGFSS HAEGNHTSTAHFAGSHIMGRFGTAEESYSWFIANGTNETDHNIGAKWLAHNGEMYIDGAS YNASGTDFAQMFEAVDNTLIDVGYFVTFSSEEKIRIATSNDSFILGISSATPALIGNSGA LSWQKRYKTDSFGKRQYVRTESQDIQPLLNTEWDPACKYIARKDRTEWLPVGLIGQMLVR DDGTCKTHGYCRPNDKGIATKSESGFFVIKRTGDNQILILFR
      A0A0K6MGG5_BACIU
      Icd 664 358
      N.A. N.A.
      1269
      423
      P39126
      423
      icd
      4.7444
      46417.77
      224308
      Bacillus subtilis (strain 168)
      Icd
      Isocitrate dehydrogenase [NADP]
      Icd
      MAQGEKITVSNGVLNVPNNPIIPFIEGDGTGPDIWNAASKVLEAAVEKAYKGEKKITWKE VYAGEKAYNKTGEWLPAETLDVIREYFIAIKGPLTTPVGGGIRSLNVALRQELDLFVCLR PVRYFTGVPSPVKRPEDTDMVIFRENTEDIYAGIEYAKGSEEVQKLISFLQNELNVNKIR FPETSGIGIKPVSEEGTSRLVRAAIDYAIEHGRKSVTLVHKGNIMKFTEGAFKNWGYELA EKEYGDKVFTWAQYDRIAEEQGKDAANKAQSEAEAAGKIIIKDSIADIFLQQILTRPNEF DVVATMNLNGDYISDALAAQVGGIGIAPGANINYETGHAIFEATHGTAPKYAGLDKVNPS SVILSGVLLLEHLGWNEAADLVIKSMEKTIASKVVTYDFARLMDGATEVKCSEFGEELIK NMD
      IDH_BACSU
      IlvC 433 407
      N.A. N.A.
      1026
      342
      A0A0K6MM04
      336
      ilvC_1
      5.0436
      36678.64
      1423
      Bacillus subtilis
      IlvC
      Ketol-acid reductoisomerase
      IlvC
      MAKVYYEKDVTVNVLKEKKVAIIGYGSQGHAHAQNLRDNGFDVVVGLRKGKSWDKAKEDG FSVYTVAEAAKQADVVMILLPDELQPEVYEAEIAPNLQAGNSLVFAHGFNVHFDQVKPPV NVDVFLVAPKGPGHLVRRTFSEGGAVPALFAVYQDATGVATEKALSYADGIGATRAGVLE TTFKEETETDLFGEQAVLCGGVTALVKAGFETLVDAGYQPELAYFECLHELKLIVDLMYE GGLENMRYSVSDTAQWGDFVSGPRVVTEDTKKAMGAVLAEIQDGTFARGWIAEHKAGRPN FHATNEKENEHEIEVVGRKLREMMPFVQPRVKAGVK
      A0A0K6MM04_BACIU
      KatA 203 259
      N.A. N.A.
      1449
      483
      P26901
      483
      Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.
      katA
      6.5104
      54791.29
      224308
      Bacillus subtilis (strain 168)
      KatA
      Vegetative catalase
      KatA
      MSSNKLTTSWGAPVGDNQNSMTAGSRGPTLIQDVHLLEKLAHFNRERVPERVVHAKGAGA HGYFEVTNDVTKYTKAAFLSEVGKRTPLFIRFSTVAGELGSADTVRDPRGFAVKFYTEEG NYDIVGNNTPVFFIRDAIKFPDFIHTQKRDPKTHLKNPTAVWDFWSLSPESLHQVTILMS DRGIPATLRHMHGFGSHTFKWTNAEGEGVWIKYHFKTEQGVKNLDVNTAAKIAGENPDYH TEDLFNAIENGDYPAWKLYVQIMPLEDANTYRFDPFDVTKVWSQKDYPLIEVGRMVLDRN PENYFAEVEQATFSPGTLVPGIDVSPDKMLQGRLFAYHDAHRYRVGANHQALPINRARNK VNNYQRDGQMRFDDNGGGSVYYEPNSFGGPKESPEDKQAAYPVQGIADSVSYDHYDHYTQ AGDLYRLMSEDERTRLVENIVNAMKPVEKEEIKLRQIEHFYKADPEYGKRVAEGLGLPIK KDS
      CATA_BACSU
      Mdh 691 446
      N.A. N.A.
      936
      312
      P49814
      312
      Catalyzes the reversible oxidation of malate to oxaloacetate.
      mdh
      4.6439
      33643.53
      224308
      Bacillus subtilis (strain 168)
      Mdh
      Malate dehydrogenase
      Mdh
      MGNTRKKVSVIGAGFTGATTAFLIAQKELADVVLVDIPQLENPTKGKALDMLEASPVQGF DAKITGTSNYEDTAGSDIVVITAGIARKPGMSRDDLVSTNEKIMRSVTQEIVKYSPDSII VVLTNPVDAMTYAVYKESGFPKERVIGQSGVLDTARFRTFVAEELNLSVKDVTGFVLGGH GDDMVPLVRYSYAGGIPLETLIPKERIDAIVERTRKGGGEIVNLLGNGSAYYAPAASLTE MVEAILKDQRRVLPTIAYLEGEYGYEGIYLGVPTIVGGNGLEQIIELELTDYERAQLNKS VESVKNVMKVLS
      MDH_BACSU
      Pgk 674 348
      N.A. N.A.
      1182
      394
      P40924
      394
      pgk
      4.7054
      42190.29
      224308
      Bacillus subtilis (strain 168)
      Pgk
      Phosphoglycerate kinase
      Pgk
      MNKKTLKDIDVKGKVVFCRVDFNVPMKDGEVTDDTRIRAALPTIKHLADQGAKVLLASHL GRPKGEVVEELRLTPVAARLGELLGKEVKKADEAYGDAVKAQISEMKDGDVLVLENVRFY PGEEKNDPELAKAFAELADVYVNDAFGAAHRAHASTAGIAEHLPAVAGFLMEKELDVLGK AVSNPDRPFTAIIGGAKVKDKIGVIESLLDKVDNLIIGGGLAYTFVKALGYEVGKSLLEE DKIELAKSFMDRAKEKGVNFYMPEDVLVADDFSNDANVKIVPISEIPSDLEAIDIGTKTR ETYADVIKNSKLVVWNGPMGVFEIDLFAQGTKAVAEALAEAKDTYSVIGGGDSAAAVEKF GLADKMSHISTGGGASLEFMEGKELPGVAALNDK
      PGK_BACSU
      PtsH 676 997
      N.A. N.A.
      264
      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:protein serine/threonine kinase activity [GO:0004674]
      • P:phosphoenolpyruvate-dependent sugar phosphotransferase system [GO:0009401]
      • P:regulation of carbohydrate utilization [GO:0043610]
      • P:regulation of transcription, DNA-templated [GO:0006355]
      • P:transcription, DNA-templated [GO:0006351]
      4.5183
      9189.36
      224308
      Bacillus subtilis (strain 168)
      PtsH
      Phosphocarrier protein HPr
      PtsH
      MAQKTFKVTADSGIHARPATVLVQTASKYDADVNLEYNGKTVNLKSIMGVMSLGIAKGAE ITISASGADENDALNALEETMKSEGLGE
      PTHP_BACSU
      RsbW 870 775
      N.A. N.A.
      480
      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
      4.231
      17993.0
      224308
      Bacillus subtilis (strain 168)
      RsbW
      Serine-protein kinase RsbW
      RsbW
      MKNNADYIEMKVPAQPEYVGIIRLTLSGVASRMGYTYDEIEDLKIAVSEACTNAVQHAYK EDKNGEVSIRFGVFEDRLEVIVADEGDSFDFDQKQQDLGPYTPSHTVDQLSEGGLGLYLM ETLMDEVRVQNHSGVTVAMTKYLNGERVDHDTTIKNYETN
      RSBW_BACSU
      SodA 608 665
      N.A. N.A.
      606
      202
      P54375
      202
      Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
      sodA
      5.0621
      22489.95
      224308
      Bacillus subtilis (strain 168)
      SodA
      Superoxide dismutase [Mn]
      SodA
      MAYELPELPYAYDALEPHIDKETMTIHHTKHHNTYVTNLNKAVEGNTALANKSVEELVAD LDSVPENIRTAVRNNGGGHANHKLFWTLLSPNGGGEPTGALAEEINSVFGSFDKFKEQFA AAAAGRFGSGWAWLVVNNGKLEITSTPNQDSPLSEGKTPILGLDVWEHAYYLNYQNRRPD YISAFWNVVNWDEVARLYSEAK
      SODM_BACSU
      YdbD 644 513
      N.A. N.A.
      819
      273
      unknown
      P80878
      273
      ydbD
      4.7873
      30257.37
      224308
      Bacillus subtilis (strain 168)
      YdbD
      Probable manganese catalase
      YdbD
      MFKHTKMLQHPAKPDRPDPLFAKKMQEILGGQFGEISVAMQYLFQGWNTRGNEKYKDLLM DTATEELGHVEMIATMIARLLEDAPLDQQEKAAEDPVIGSILGGMNPHHAIVSGLGAMPE SSTGVPWSGGYIVASGNLLADFRANLNAESQGRLQVARLFEMTDDKGVKDMLSFLLARDT MHQNQWLAAIKELEAQEGPVVPGTFPKALEKQEFSHQLINFSEGEVSAEQNWLNEKAPDG EAFEYVKEAKTFGEKPELKPAPPFVHNTLPGRE
      MCAT_BACSU
      YtxH 565 743
      N.A. N.A.
      456
      152
      unknown
      P40780
      151
      ytxH
        5.0714
        16554.59
        224308
        Bacillus subtilis (strain 168)
        YtxH
        Uncharacterized protein YtxH
        YtxH
        MSKDGINSKDFLIGTLIGGIIGATTALFLAPKSGKELRDDLGSQAVALRDKTDKMTADAK EKGTQYVSIAKDKTSNITQLVADQSGQIMNKVKDLRDRSKSDKTDSSTAMQDMREEAMQA ADETKDQVLQTKEDVKDELKDAQKQAEQLNR
        YTXH_BACSU
        YvyD 518 622
        N.A. N.A.
        567
        189
        unknown
        G4P1B5
        189
        raiA
        5.3935
        21950.72
        1052585
        Bacillus subtilis subsp. spizizenii (strain TU-B-10)
        YvyD
        YvyD
        MNYNIRGENIEVTPALKDHVEKKIGKLERYFDHSVNADVNVNLKFYNDKESKVEVTIPMT DLALRSEVHNEDMYNAIDLATNKLERQIRKHKTKVNRKFREQGSPKYLLANGLGSDTDIA VQDEIEDEESLDIVRQKRFNLKPMDSEEAILQMNMLGHNFFVFTNAETNLTNVVYRRNDG KYGLIEPTE
        G4P1B5_BACPT

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