ECOLI:CPXA

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	cpxA (synonyms: ecfB, eup, ssd)
Protein Name(s)	Sensor protein CpxA
External Links
UniProt	P0AE82
EMBL	M13493 M36795 X13307 L19201 U00096 AP009048
PIR	S40855
RefSeq	NP_418347.1 YP_491539.1
PDB	4BIU 4BIV 4BIW 4BIX 4BIY 4BIZ 4CB0
PDBsum	4BIU 4BIV 4BIW 4BIX 4BIY 4BIZ 4CB0
ProteinModelPortal	P0AE82
SMR	P0AE82
DIP	DIP-48358N
IntAct	P0AE82
STRING	511145.b3911
EnsemblBacteria	AAC76893 BAE77398
GeneID	12933650 948405
KEGG	ecj:Y75_p3275 eco:b3911
PATRIC	32123335
EchoBASE	EB0161
EcoGene	EG10163
eggNOG	COG0642
HOGENOM	HOG000269851
InParanoid	P0AE82
KO	K07640
OMA	IPVEKAC
OrthoDB	EOG6G4VQG
PhylomeDB	P0AE82
BioCyc	EcoCyc:CPXA-MONOMER ECOL316407:JW3882-MONOMER
PRO	PR:P0AE82
Proteomes	UP000000318 UP000000625
Genevestigator	P0AE82
GO	GO:0016021 GO:0005886 GO:0005524 GO:0000155 GO:0043708 GO:0000160 GO:0046777 GO:0023014
Gene3D	1.10.287.130 3.30.565.10
InterPro	IPR003661 IPR003660 IPR003594 IPR004358 IPR005467 IPR009082
Pfam	PF00672 PF02518 PF00512
PRINTS	PR00344
SMART	SM00304 SM00387 SM00388
SUPFAM	SSF47384 SSF55874
PROSITE	PS50885 PS50109

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0004673	protein histidine kinase activity	PMID:9401031^[1]	ECO:0000315			F	Table 7b: MBP-CpxA has protein phosphatase activity dependent on the presence of ATP and Mg, characteristic of histidine kinases	complete
	GO:0000155	phosphorelay sensor kinase activity	PMID:16176121^[2]	ECO:0001202			F	Figure 4 (G&H) Phosphorelay sensor kinase Escherichia coli (strain K12) CpxA; phosophorelay sensor histidine kinase. Histidine kinase member of the two-component regulatory system CpxA/CpxR	complete CACAO 13754
involved_in	GO:0043708	cell adhesion involved in biofilm formation	PMID:10483736^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	PMID:21873635^[4]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10163 PANTHER:PTN002557430	C	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:21873635^[4]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10163 PANTHER:PTN002557430	C	Seeded From UniProt	complete
enables	GO:0000155	phosphorelay sensor kinase activity	PMID:21873635^[4]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10163 PANTHER:PTN002557430	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:24492262^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0AE82	F	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:20081027^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0046777	protein autophosphorylation	PMID:15522865^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0023014	signal transduction by protein phosphorylation	PMID:7883164^[8]	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^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	PMID:3058985^[9]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0009314	response to radiation	PMID:27718375^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:17309111^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:15919996^[12]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0000155	phosphorelay sensor kinase activity	PMID:7883164^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000155	phosphorelay sensor kinase activity	PMID:15522865^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	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:IPR003661 InterPro:IPR036097	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: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
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: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: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: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:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C	Seeded From UniProt	complete
involved_in	GO:0007155	cell adhesion	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0130	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
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: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
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: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
	GO:0043708	cell adhesion involved in biofilm formation	PMID:10483736^[3]	ECO:0000315			P	Figure 1. shows that cpxA negative mutants showed a polystyrene adherence defect.	complete CACAO 6048
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Notes

References

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

↑ Raivio, TL & Silhavy, TJ (1997) Transduction of envelope stress in Escherichia coli by the Cpx two-component system. J. Bacteriol. 179 7724-33 PubMed GONUTS page
↑ 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
↑ ^3.0 ^3.1 Dorel, C et al. (1999) Involvement of the Cpx signal transduction pathway of E. coli in biofilm formation. FEMS Microbiol. Lett. 178 169-75 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Mechaly, AE et al. (2014) Segmental helical motions and dynamical asymmetry modulate histidine kinase autophosphorylation. PLoS Biol. 12 e1001776 PubMed GONUTS page
↑ Arutyunov, D et al. (2010) F plasmid TraF and TraH are components of an outer membrane complex involved in conjugation. J. Bacteriol. 192 1730-4 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 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
↑ ^8.0 ^8.1 Danese, PN et al. (1995) The Cpx two-component signal transduction pathway of Escherichia coli regulates transcription of the gene specifying the stress-inducible periplasmic protease, DegP. Genes Dev. 9 387-98 PubMed GONUTS page
↑ Weber, RF & Silverman, PM (1988) The cpx proteins of Escherichia coli K12. Structure of the cpxA polypeptide as an inner membrane component. J. Mol. Biol. 203 467-78 PubMed GONUTS page
↑ Sargentini, NJ et al. () Screen for genes involved in radiation survival of Escherichia coli and construction of a reference database. Mutat. Res. 793-794 1-14 PubMed GONUTS page
↑ Zhang, N et al. (2007) Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS. Proteomics 7 484-93 PubMed GONUTS page
↑ Daley, DO et al. (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science 308 1321-3 PubMed GONUTS page

[PMID:9401031-1] Raivio, TL & Silhavy, TJ (1997) Transduction of envelope stress in Escherichia coli by the Cpx two-component system. J. Bacteriol. 179 7724-33 PubMed GONUTS page

[PMID:16176121-2] 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

[PMID:10483736-3] 3.0 ^3.1 Dorel, C et al. (1999) Involvement of the Cpx signal transduction pathway of E. coli in biofilm formation. FEMS Microbiol. Lett. 178 169-75 PubMed GONUTS page

[PMID:21873635-4] 4.0 ^4.1 ^4.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:24492262-5] Mechaly, AE et al. (2014) Segmental helical motions and dynamical asymmetry modulate histidine kinase autophosphorylation. PLoS Biol. 12 e1001776 PubMed GONUTS page

[PMID:20081027-6] Arutyunov, D et al. (2010) F plasmid TraF and TraH are components of an outer membrane complex involved in conjugation. J. Bacteriol. 192 1730-4 PubMed GONUTS page

[PMID:15522865-7] 7.0 ^7.1 ^7.2 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

[PMID:7883164-8] 8.0 ^8.1 Danese, PN et al. (1995) The Cpx two-component signal transduction pathway of Escherichia coli regulates transcription of the gene specifying the stress-inducible periplasmic protease, DegP. Genes Dev. 9 387-98 PubMed GONUTS page

[PMID:3058985-9] Weber, RF & Silverman, PM (1988) The cpx proteins of Escherichia coli K12. Structure of the cpxA polypeptide as an inner membrane component. J. Mol. Biol. 203 467-78 PubMed GONUTS page

[PMID:27718375-10] Sargentini, NJ et al. () Screen for genes involved in radiation survival of Escherichia coli and construction of a reference database. Mutat. Res. 793-794 1-14 PubMed GONUTS page

[PMID:17309111-11] Zhang, N et al. (2007) Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS. Proteomics 7 484-93 PubMed GONUTS page

[PMID:15919996-12] Daley, DO et al. (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science 308 1321-3 PubMed GONUTS page

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ECOLI:CPXA

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