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ECOLI:CHEA

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) cheA
Protein Name(s) Chemotaxis protein CheA
External Links
UniProt P07363
EMBL M34669
M34669
U00096
AP009048
M13462
PIR H64951
RefSeq NP_416402.1
YP_490150.1
PDB 1A0O
1EAY
1FFG
1FFS
1FFW
1FWP
2LP4
PDBsum 1A0O
1EAY
1FFG
1FFS
1FFW
1FWP
2LP4
DisProt DP00407
ProteinModelPortal P07363
SMR P07363
DIP DIP-6053N
IntAct P07363
MINT MINT-1312842
STRING 511145.b1888
PaxDb P07363
PRIDE P07363
EnsemblBacteria AAC74958
BAA15709
GeneID 12932040
946401
KEGG ecj:Y75_p1864
eco:b1888
PATRIC 32119103
EchoBASE EB0144
EcoGene EG10146
eggNOG COG0643
HOGENOM HOG000255263
InParanoid P07363
KO K03407
OMA VQTIRVN
OrthoDB EOG62RS8P
PhylomeDB P07363
BioCyc EcoCyc:CHEA-SMALL
EcoCyc:PROTEIN-CHEA
ECOL316407:JW1877-MONOMER
RETL1328306-WGS:GSTH-3589-MONOMER
BRENDA 2.7.13.3
EvolutionaryTrace P07363
PRO PR:P07363
Proteomes UP000000318
UP000000625
Genevestigator P07363
GO GO:0005737
GO:0005829
GO:0005886
GO:0005524
GO:0000155
GO:0006935
GO:0051649
GO:0031400
GO:0000160
GO:0016310
GO:0035307
GO:0046777
Gene3D 1.10.287.560
1.20.120.160
3.30.565.10
3.30.70.400
InterPro IPR004105
IPR002545
IPR015162
IPR003594
IPR004358
IPR008207
IPR005467
IPR009082
Pfam PF01584
PF09078
PF02895
PF02518
PF01627
PRINTS PR00344
SMART SM00260
SM00387
SM00073
SUPFAM SSF47226
SSF47384
SSF50341
SSF55052
SSF55874
PROSITE PS50851
PS50109
PS50894

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0005737

cytoplasm

PMID:334749[1]

ECO:0000314

C

table 4 and fig 2,3,4

complete

GO:0005886

plasma membrane

PMID:334749[1]

ECO:0000314

C

table 4 and fig 2,3,4

complete

GO:0000155

phosphorelay sensor kinase activity

PMID:16176121[2]

ECO:0001202

F

Figure 4 (E&F) Phosphorelay histidine sensor kinase Escherichia coli CheA. Sensory histidine kinase member of two-component regulatory system with CheB and CheY

complete
CACAO 13760

involved_in

GO:1902021

regulation of bacterial-type flagellum-dependent cell motility

PMID:18931127[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0050920

regulation of chemotaxis

PMID:18931127[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

PMID:18931127[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0098561

methyl accepting chemotaxis protein complex

PMID:18931127[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004673

protein histidine kinase activity

PMID:18931127[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

GO:0006935

chemotaxis

PMID:11295559[4]

ECO:0000021

EcoCyc:EG10146 EcoCyc:b1888


P

Figure1. two-component signal transduction complex

complete

involved_in

GO:1901875

positive regulation of post-translational protein modification

PMID:15916610[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

GO:0031400

negative regulation of protein modification process

PMID:15327941[6]

ECO:0000314

P

Figure 1A. Presence of CheA negatively regulates acetylation of CheY.

complete
CACAO 5148

part_of

GO:0005886

plasma membrane

PMID:15916610[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0098561

methyl accepting chemotaxis protein complex

PMID:15916610[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0031400

negative regulation of protein modification process

PMID:15327941[6]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0046777

protein autophosphorylation

PMID:2558046[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0016310

phosphorylation

PMID:2558046[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0000160

phosphorelay signal transduction system

PMID:2558046[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0051649

establishment of localization in cell

PMID:12644507[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0051649

establishment of localization in cell

PMID:19502407[9]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0035307

positive regulation of protein dephosphorylation

PMID:8820640[10]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0023014

signal transduction by protein phosphorylation

PMID:2558046[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006935

chemotaxis

PMID:8820640[10]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

PMID:334749[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:334749[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:334749[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0018106

peptidyl-histidine phosphorylation

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0004673

P

Seeded From UniProt

complete

involved_in

GO:0018106

peptidyl-histidine phosphorylation

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0004673

P

Seeded From UniProt

complete

involved_in

GO:0018106

peptidyl-histidine phosphorylation

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0004673

P

Seeded From UniProt

complete

enables

GO:0000155

phosphorelay sensor kinase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004105
InterPro:IPR036097
InterPro:IPR037006

F

Seeded From UniProt

complete

involved_in

GO:0000160

phosphorelay signal transduction system

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004105
InterPro:IPR008207
InterPro:IPR036641

P

Seeded From UniProt

complete

enables

GO:0004673

protein histidine kinase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004105

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004105

C

Seeded From UniProt

complete

involved_in

GO:0006935

chemotaxis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002545
InterPro:IPR004105
InterPro:IPR036061
InterPro:IPR037006

P

Seeded From UniProt

complete

involved_in

GO:0007165

signal transduction

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002545
InterPro:IPR036061
InterPro:IPR036097

P

Seeded From UniProt

complete

involved_in

GO:0016310

phosphorylation

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004358

P

Seeded From UniProt

complete

enables

GO:0016772

transferase activity, transferring phosphorus-containing groups

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004358

F

Seeded From UniProt

complete

enables

GO:0004673

protein histidine kinase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.7.13.3

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

involved_in

GO:0016310

phosphorylation

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0418

P

Seeded From UniProt

complete

enables

GO:0016301

kinase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0418

F

Seeded From UniProt

complete

involved_in

GO:0006935

chemotaxis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0145

P

Seeded From UniProt

complete

involved_in

GO:0000160

phosphorelay signal transduction system

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0902

P

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 1.3 1.4 Ridgway, HG et al. (1977) Localization of proteins controlling motility and chemotaxis in Escherichia coli. J. Bacteriol. 132 657-65 PubMed GONUTS page
  2. Skerker, JM et al. (2005) Two-component signal transduction pathways regulating growth and cell cycle progression in a bacterium: a system-level analysis. PLoS Biol. 3 e334 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 3.4 Mowery, P et al. (2008) Different signaling roles of two conserved residues in the cytoplasmic hairpin tip of Tsr, the Escherichia coli serine chemoreceptor. J. Bacteriol. 190 8065-74 PubMed GONUTS page
  4. Falke, JJ & Hazelbauer, GL (2001) Transmembrane signaling in bacterial chemoreceptors. Trends Biochem. Sci. 26 257-65 PubMed GONUTS page
  5. 5.0 5.1 5.2 Li, M & Hazelbauer, GL (2005) Adaptational assistance in clusters of bacterial chemoreceptors. Mol. Microbiol. 56 1617-26 PubMed GONUTS page
  6. 6.0 6.1 Barak, R & Eisenbach, M (2004) Co-regulation of acetylation and phosphorylation of CheY, a response regulator in chemotaxis of Escherichia coli. J. Mol. Biol. 342 375-81 PubMed GONUTS page
  7. 7.0 7.1 7.2 7.3 Igo, MM et al. (1989) Phosphorylation and dephosphorylation of a bacterial transcriptional activator by a transmembrane receptor. Genes Dev. 3 1725-34 PubMed GONUTS page
  8. Cantwell, BJ et al. (2003) CheZ phosphatase localizes to chemoreceptor patches via CheA-short. J. Bacteriol. 185 2354-61 PubMed GONUTS page
  9. Hao, S et al. (2009) Structural basis for the localization of the chemotaxis phosphatase CheZ by CheAS. J. Bacteriol. 191 5842-4 PubMed GONUTS page
  10. 10.0 10.1 Wang, H & Matsumura, P (1996) Characterization of the CheAS/CheZ complex: a specific interaction resulting in enhanced dephosphorylating activity on CheY-phosphate. Mol. Microbiol. 19 695-703 PubMed GONUTS page