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ECOLI:PHOQ

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) phoQ
Protein Name(s) Sensor protein PhoQ

Sensor histidine protein kinase/phosphatase PhoQ

External Links
UniProt P23837
EMBL D90393
U00096
AP009048
M81433
PIR B41966
RefSeq NP_415647.1
YP_489397.1
PDB 1ID0
3BQ8
3BQA
PDBsum 1ID0
3BQ8
3BQA
ProteinModelPortal P23837
SMR P23837
DIP DIP-10501N
IntAct P23837
STRING 511145.b1129
PaxDb P23837
PRIDE P23837
EnsemblBacteria AAC74213
BAA35951
GeneID 12931668
946326
KEGG ecj:Y75_p1099
eco:b1129
PATRIC 32117507
EchoBASE EB0725
EcoGene EG10732
eggNOG COG0642
HOGENOM HOG000274481
InParanoid P23837
KO K07637
OMA AHWSLRP
OrthoDB EOG6G4VQG
PhylomeDB P23837
BioCyc EcoCyc:PHOQ-MONOMER
ECOL316407:JW1115-MONOMER
BRENDA 2.7.13.3
EvolutionaryTrace P23837
PRO PR:P23837
Proteomes UP000000318
UP000000625
Genevestigator P23837
GO GO:0016021
GO:0005886
GO:0005524
GO:0046872
GO:0004721
GO:0000155
GO:0010350
GO:0000160
GO:0046777
GO:0023014
Gene3D 3.30.565.10
InterPro IPR003661
IPR003660
IPR003594
IPR015014
IPR004358
IPR005467
IPR009082
Pfam PF00672
PF02518
PF08918
PRINTS PR00344
SMART SM00387
SM00388
SUPFAM SSF47384
SSF55874
PROSITE PS50885
PS50109

Annotations

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

part_of

GO:0005886

plasma membrane

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10732
EcoGene:EG11614
EcoGene:EG13027
EcoGene:EG13642
EcoGene:EG14044
PANTHER:PTN001976770
UniProtKB:O69729

C

Seeded From UniProt

complete

involved_in

GO:0000160

phosphorelay signal transduction system

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001976770
UniProtKB:Q9HV31

P

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:25087511[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P23837

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:20404199[3]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P23837

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

PMID:18348979[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0046777

protein autophosphorylation

PMID:15522865[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0046777

protein autophosphorylation

PMID:16041131[6]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0023014

signal transduction by protein phosphorylation

PMID:10464230[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0023014

signal transduction by protein phosphorylation

PMID:15522865[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0016301

kinase activity

PMID:16041131[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0010350

cellular response to magnesium starvation

PMID:10464230[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005887

integral component of plasma membrane

PMID:1729240[8]

ECO:0000255

match to sequence model evidence used in manual assertion

C

Seeded From UniProt

Missing: with/from

part_of

GO:0005886

plasma membrane

PMID:15919996[9]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004721

phosphoprotein phosphatase activity

PMID:27447896[10]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000155

phosphorelay sensor kinase activity

PMID:10464230[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006470

protein dephosphorylation

GO_REF:0000108

ECO:0000364

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

GO:0004721

P

Seeded From UniProt

complete

involved_in

GO:0006470

protein dephosphorylation

GO_REF:0000108

ECO:0000366

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

GO:0004721

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:IPR003661
InterPro:IPR036097

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:IPR015014

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:IPR015014

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR015014

F

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:IPR003660
InterPro:IPR003661
InterPro:IPR036097

P

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR015014

C

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003660

C

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

involved_in

GO:0018106

peptidyl-histidine phosphorylation

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR015014

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR015014

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

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

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

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1003
UniProtKB-KW:KW-0997
UniProtKB-SubCell:SL-0037

C

Seeded From UniProt

complete

enables

GO:0004721

phosphoprotein phosphatase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0904

F

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

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

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

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: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: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

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

edit table

Notes

References

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

  1. ↑ 1.0 1.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  2. ↑ Molnar, KS et al. (2014) Cys-scanning disulfide crosslinking and bayesian modeling probe the transmembrane signaling mechanism of the histidine kinase, PhoQ. Structure 22 1239-1251 PubMed GONUTS page
  3. ↑ Goldberg, SD et al. (2010) Transmembrane polar interactions are required for signaling in the Escherichia coli sensor kinase PhoQ. Proc. Natl. Acad. Sci. U.S.A. 107 8141-6 PubMed GONUTS page
  4. ↑ Cheung, J et al. (2008) Crystal structure of a functional dimer of the PhoQ sensor domain. J. Biol. Chem. 283 13762-70 PubMed GONUTS page
  5. ↑ 5.0 5.1 Yamamoto, K et al. (2005) Functional characterization in vitro of all two-component signal transduction systems from Escherichia coli. J. Biol. Chem. 280 1448-56 PubMed GONUTS page
  6. ↑ 6.0 6.1 Minagawa, S et al. (2005) Isolation and molecular characterization of the locked-on mutant of Mg2+ sensor PhoQ in Escherichia coli. Biosci. Biotechnol. Biochem. 69 1281-7 PubMed GONUTS page
  7. ↑ 7.0 7.1 7.2 Kato, A et al. (1999) Molecular characterization of the PhoP-PhoQ two-component system in Escherichia coli K-12: identification of extracellular Mg2+-responsive promoters. J. Bacteriol. 181 5516-20 PubMed GONUTS page
  8. ↑ Kasahara, M et al. (1992) Molecular analysis of the Escherichia coli phoP-phoQ operon. J. Bacteriol. 174 492-8 PubMed GONUTS page
  9. ↑ Daley, DO et al. (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science 308 1321-3 PubMed GONUTS page
  10. ↑ Salazar, ME et al. (2016) The small membrane protein MgrB regulates PhoQ bifunctionality to control PhoP target gene expression dynamics. Mol. Microbiol. 102 430-445 PubMed GONUTS page
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