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

control_01	control
	control_01
Spot	Pi/MW Estimation	Label name(s)	GenoList	Uniprot	AureoList
ID	Pi	MW		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)
13019	4.72	81255
13286	5.70	37190	CysK	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
13562	5.13	30176
13575	4.95	25420	SodA	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
13694	4.67	73928	AhpF	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
13721	4.46	61315	Eno	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
13817	5.45	94983
13840	5.07	126377
13886	4.55	96239	DnaK	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
13911	4.56	86569	GroEL	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

control_01

control

control_01

Spot

Pi/MW Estimation

Label name(s)

GenoList

Uniprot

AureoList

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)

13019

4.72

81255

13286

5.70

37190

CysK

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

13562

5.13

30176

13575

4.95

25420

SodA

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

13694

4.67

73928

AhpF

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

13721

4.46

61315

Eno

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

13817

5.45

94983

13840

5.07

126377

13886

4.55

96239

DnaK

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

13911

4.56

86569

GroEL

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

Delta2D Labelsfor Project 'Demonstration'

Labels

Delta2D Labels
for Project 'Demonstration'