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Protein

Sensor histidine kinase CpxA

Gene

cpxA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Histidine kinase member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating expression of downstream genes including cpxP, degP, dsbA and ppiA (PubMed:7883164, PubMed:9401031, PubMed:9473036). Activates CpxR by phosphorylation; has autokinase, phosphotransferase and (in the presence of Mg2+ and/or ATP or ADP) phosphatase activity (PubMed:9401031, PubMed:17259177, PubMed:24492262). The kinase activity is inhibited by periplasmic accessory protein CpxP; proteolysis of CpxP relieves inhibition (PubMed:16166523, PubMed:17259177, PubMed:25207645). Involved in several diverse cellular processes, including the functioning of acetohydroxyacid synthetase I, the biosynthesis of isoleucine and valine, the TraJ protein activation activity for tra gene expression in F plasmid (PubMed:8432716), and the synthesis, translocation, or stability of cell envelope proteins (PubMed:7883164). Activates transcription of periplasmic protease degP, probably by phosphorylating the cognate response protein CpxR; overexpression of an outer membrane lipoprotein NlpE also leads to transcription of degP via CpxRA (PubMed:7883164).8 Publications

Catalytic activityi

ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.1 Publication

Cofactori

Mg2+1 PublicationNote: Phosphotransfer to CpxR is stimulated by Mg2+ and/or Mn2+.1 Publication

Enzyme regulationi

The two-component system is activated by envelope stress such as overexpression of some (misfolded) periplasmic proteins (PubMed:7883164, PubMed:9351822). Activated by spheroplasting (which removes the periplasm) in an autoregulatory cpxA-cpxR-dependent fashion (PubMed:10972835). Cpx two-component system is induced at pH 8.0; in a degP deletion mutant induction is halved (PubMed:9473036, PubMed:16166523). The kinase activity is inhibited by periplasmic accessory protein CpxP; proteolysis of CpxP relieves inhibition (PubMed:16166523, PubMed:17259177, PubMed:25207645). Autokinase activity reconstituted in liposomes is 50% inhibited by periplasmic accessory protein CpxP, but CpxP has no effect on phosphatase activity; autokinase stimulated by KCl, NH4Cl, RbCl, pH 7.5 and 8.0, inhibited by sensor kinase inhibitors tetrachlorosalicylanilid and ethodin (PubMed:17259177).7 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei248 – 2481Nucleophile1 Publication
Binding sitei248 – 2481ATP1 Publication
Binding sitei386 – 3861ATP1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi248 – 2514ATP1 Publication
Nucleotide bindingi359 – 3646ATP1 Publication
Nucleotide bindingi405 – 4062ATP1 Publication
Nucleotide bindingi416 – 4216ATP1 Publication

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • phosphorelay sensor kinase activity Source: EcoCyc

GO - Biological processi

  • cell adhesion involved in biofilm formation Source: CACAO
  • phosphorelay signal transduction system Source: EcoCyc
  • protein autophosphorylation Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Two-component regulatory system

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:CPXA-MONOMER.
ECOL316407:JW3882-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Sensor histidine kinase CpxA (EC:2.7.13.31 Publication)
Gene namesi
Name:cpxA
Synonyms:ecfB, eup, ssd
Ordered Locus Names:b3911, JW3882
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10163. cpxA.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 77Cytoplasmic1 Publication
Transmembranei8 – 2922HelicalCuratedAdd
BLAST
Topological domaini30 – 163134Periplasmic2 PublicationsAdd
BLAST
Transmembranei164 – 18421HelicalCuratedAdd
BLAST
Topological domaini185 – 457273Cytoplasmic2 PublicationsAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: EcoCyc
  • intracellular Source: GOC
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Loss of the Cpx envelope stress response (PubMed:10972835). Decreased resistance to the antibiotic amnikacin (PubMed:2185221). Single cpxA and double cpxR-cpxA mutant decrease transcription of degP (PubMed:7883164). Decreased transcription of cpxP (PubMed:9473036). Hypersensitive to alkaline pH (greater than pH 8.8) (PubMed:9473036). Greatly increased resistance to hydroxyurea, probably due to decreased recognition of mis-folded proteins which eventually leads to decreased OH radical formation (PubMed:20005847).5 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi33 – 331R → C in cpxA104; a cpxA gain of function mutant, constitutively active. 1 Publication
Mutagenesisi93 – 12432Missing in cpxA24; a cpxA gain of function mutant, constitutively active, up-regulation of the Cpx regulon members. 1 PublicationAdd
BLAST
Mutagenesisi185 – 1851S → R: Nearly complete loss of response to excess periplasmic protein. 1 Publication
Mutagenesisi186 – 1861L → Q: 30% decrease in response to excess periplasmic protein. 1 Publication
Mutagenesisi197 – 1971A → V: Slight decrease in response to excess periplasmic protein. 1 Publication
Mutagenesisi204 – 2041N → Y: 80% decrease in response to excess periplasmic protein. 1 Publication
Mutagenesisi222 – 2221G → D: 90% decrease in response to excess periplasmic protein. 1 Publication
Mutagenesisi222 – 2221G → R: 75% decrease in response to excess periplasmic protein. 1 Publication
Mutagenesisi228 – 2281M → V: No response to excess periplasmic protein, decreased autophosphorylation, no phosphotransfer to CpxR, no tetramer formation of the C-terminal domain in solution. 1 Publication
Mutagenesisi252 – 2521T → P in cpxA101; a cpxA gain of function mutant, decreased autophosphorylation, decreased phosphotransfer to CpxR, loss of phosphatase activity, responds to periplasmic protein overproduction. 1 Publication
Mutagenesisi356 – 3561N → Y: Nearly complete loss of response to excess periplasmic protein. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 457457Sensor histidine kinase CpxAPRO_0000074739Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei248 – 2481Phosphohistidine; by autocatalysisPROSITE-ProRule annotation2 Publications

Post-translational modificationi

Autophosphorylated (PubMed:9401031, PubMed:24492262). Maximal phosphorylation of the dimeric isolated cytoplasmic domain (residues 188-457) is about 70%, suggesting the protein may be hemiphosphorylated in vivo; probably occurs via a trans-autophosphorylation mechanism, i.e. one subunit phopshorylates the other (PubMed:24492262).2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP0AE82.

PTM databases

iPTMnetiP0AE82.

Interactioni

Subunit structurei

The isolated cytoplasmic domain (residues 188-457) crystallizes as a homodimer, and forms dimers of dimers in solution which may be catalytically important (PubMed:24492262). Interacts with periplasmic accessory protein CpxP (PubMed:16166523, PubMed:21317318, PubMed:21239493, PubMed:25207645); interaction with CpxP is not seen in vivo when cells are grown in 0.3 M NaCl, or if the misfolded P pili protein PapE is overexpressed (PubMed:25207645). Interacts with cognate response regulator CpxR (PubMed:25207645).1 Publication2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
paaXP760863EBI-9141330,EBI-544692

Protein-protein interaction databases

BioGridi4262644. 12 interactions.
DIPiDIP-48358N.
IntActiP0AE82. 2 interactions.
STRINGi511145.b3911.

Structurei

Secondary structure

1
457
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi189 – 20012Combined sources
Turni201 – 2033Combined sources
Helixi209 – 2124Combined sources
Beta strandi214 – 2163Combined sources
Helixi217 – 2204Combined sources
Helixi221 – 24929Combined sources
Helixi251 – 26717Combined sources
Helixi272 – 29625Combined sources
Beta strandi299 – 3013Combined sources
Beta strandi306 – 3094Combined sources
Helixi310 – 32819Combined sources
Beta strandi331 – 3366Combined sources
Beta strandi342 – 3454Combined sources
Helixi347 – 36418Combined sources
Beta strandi366 – 37510Combined sources
Beta strandi377 – 38610Combined sources
Helixi393 – 3953Combined sources
Helixi398 – 4003Combined sources
Helixi407 – 4126Combined sources
Helixi421 – 43010Combined sources
Beta strandi434 – 4396Combined sources
Beta strandi443 – 45210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BIUX-ray3.65A/B/C/D/E/F188-457[»]
4BIVX-ray3.40A/B188-457[»]
4BIWX-ray2.85A/B188-457[»]
4BIXX-ray2.00A/B188-457[»]
4BIYX-ray3.30A/B/C/D188-457[»]
4BIZX-ray2.65A/B/C/D/E/F188-457[»]
4CB0X-ray3.30A/B188-457[»]
ProteinModelPortaliP0AE82.
SMRiP0AE82. Positions 188-456.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini185 – 23753HAMPPROSITE-ProRule annotationAdd
BLAST
Domaini245 – 455211Histidine kinasePROSITE-ProRule annotationAdd
BLAST

Domaini

The periplasmic segment (residues 30-163) defines the sensory domain (PubMed:9401031). Conformational changes in the cytoplasmic HAMP domain modulate the mobility of the central alpha-helices (which bend at Ser-238 and Pro-253) that allows formation of 1 kinase-active state.2 Publications

Sequence similaritiesi

Contains 1 HAMP domain.PROSITE-ProRule annotation
Contains 1 histidine kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105E0F. Bacteria.
ENOG410XTWD. LUCA.
HOGENOMiHOG000269851.
InParanoidiP0AE82.
KOiK07640.
OMAiIPVEKAC.
OrthoDBiEOG6G4VQG.
PhylomeDBiP0AE82.

Family and domain databases

Gene3Di1.10.287.130. 1 hit.
3.30.565.10. 1 hit.
InterProiIPR032404. CpxA_peri.
IPR003660. HAMP_dom.
IPR003594. HATPase_C.
IPR005467. His_kinase_dom.
IPR003661. HisK_dim/P.
IPR004358. Sig_transdc_His_kin-like_C.
[Graphical view]
PfamiPF16527. CpxA_peri. 1 hit.
PF00672. HAMP. 1 hit.
PF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM00304. HAMP. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
[Graphical view]
SUPFAMiSSF47384. SSF47384. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEiPS50885. HAMP. 1 hit.
PS50109. HIS_KIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AE82-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIGSLTARIF AIFWLTLALV LMLVLMLPKL DSRQMTELLD SEQRQGLMIE
60 70 80 90 100
QHVEAELAND PPNDLMWWRR LFRAIDKWAP PGQRLLLVTT EGRVIGAERS
110 120 130 140 150
EMQIIRNFIG QADNADHPQK KKYGRVELVG PFSVRDGEDN YQLYLIRPAS
160 170 180 190 200
SSQSDFINLL FDRPLLLLIV TMLVSTPLLL WLAWSLAKPA RKLKNAADEV
210 220 230 240 250
AQGNLRQHPE LEAGPQEFLA AGASFNQMVT ALERMMTSQQ RLLSDISHEL
260 270 280 290 300
RTPLTRLQLG TALLRRRSGE SKELERIETE AQRLDSMIND LLVMSRNQQK
310 320 330 340 350
NALVSETIKA NQLWSEVLDN AAFEAEQMGK SLTVNFPPGP WPLYGNPNAL
360 370 380 390 400
ESALENIVRN ALRYSHTKIE VGFAVDKDGI TITVDDDGPG VSPEDREQIF
410 420 430 440 450
RPFYRTDEAR DRESGGTGLG LAIVETAIQQ HRGWVKAEDS PLGGLRLVIW

LPLYKRS
Length:457
Mass (Da):51,624
Last modified:December 6, 2005 - v1
Checksum:i720EE4A62885BA33
GO

Sequence cautioni

The sequence AAA72540.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681W → WW in AAA23600 (PubMed:3007473).Curated
Sequence conflicti68 – 681W → WW in CAA31687 (PubMed:3058985).Curated
Sequence conflicti330 – 3301K → R in AAA23600 (PubMed:3007473).Curated
Sequence conflicti330 – 3301K → R in AAA72540 (PubMed:3007473).Curated
Sequence conflicti330 – 3301K → R in CAA31687 (PubMed:3058985).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13493 Genomic DNA. Translation: AAA72540.1. Different initiation.
M36795 Genomic DNA. Translation: AAA23600.1.
X13307 Genomic DNA. Translation: CAA31687.1.
L19201 Genomic DNA. Translation: AAB03044.1.
U00096 Genomic DNA. Translation: AAC76893.1.
AP009048 Genomic DNA. Translation: BAE77398.1.
PIRiS40855.
RefSeqiNP_418347.1. NC_000913.3.
WP_000580417.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76893; AAC76893; b3911.
BAE77398; BAE77398; BAE77398.
GeneIDi948405.
KEGGiecj:JW3882.
eco:b3911.
PATRICi32123335. VBIEscCol129921_4028.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13493 Genomic DNA. Translation: AAA72540.1. Different initiation.
M36795 Genomic DNA. Translation: AAA23600.1.
X13307 Genomic DNA. Translation: CAA31687.1.
L19201 Genomic DNA. Translation: AAB03044.1.
U00096 Genomic DNA. Translation: AAC76893.1.
AP009048 Genomic DNA. Translation: BAE77398.1.
PIRiS40855.
RefSeqiNP_418347.1. NC_000913.3.
WP_000580417.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BIUX-ray3.65A/B/C/D/E/F188-457[»]
4BIVX-ray3.40A/B188-457[»]
4BIWX-ray2.85A/B188-457[»]
4BIXX-ray2.00A/B188-457[»]
4BIYX-ray3.30A/B/C/D188-457[»]
4BIZX-ray2.65A/B/C/D/E/F188-457[»]
4CB0X-ray3.30A/B188-457[»]
ProteinModelPortaliP0AE82.
SMRiP0AE82. Positions 188-456.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262644. 12 interactions.
DIPiDIP-48358N.
IntActiP0AE82. 2 interactions.
STRINGi511145.b3911.

PTM databases

iPTMnetiP0AE82.

Proteomic databases

PaxDbiP0AE82.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76893; AAC76893; b3911.
BAE77398; BAE77398; BAE77398.
GeneIDi948405.
KEGGiecj:JW3882.
eco:b3911.
PATRICi32123335. VBIEscCol129921_4028.

Organism-specific databases

EchoBASEiEB0161.
EcoGeneiEG10163. cpxA.

Phylogenomic databases

eggNOGiENOG4105E0F. Bacteria.
ENOG410XTWD. LUCA.
HOGENOMiHOG000269851.
InParanoidiP0AE82.
KOiK07640.
OMAiIPVEKAC.
OrthoDBiEOG6G4VQG.
PhylomeDBiP0AE82.

Enzyme and pathway databases

BioCyciEcoCyc:CPXA-MONOMER.
ECOL316407:JW3882-MONOMER.

Miscellaneous databases

PROiP0AE82.

Family and domain databases

Gene3Di1.10.287.130. 1 hit.
3.30.565.10. 1 hit.
InterProiIPR032404. CpxA_peri.
IPR003660. HAMP_dom.
IPR003594. HATPase_C.
IPR005467. His_kinase_dom.
IPR003661. HisK_dim/P.
IPR004358. Sig_transdc_His_kin-like_C.
[Graphical view]
PfamiPF16527. CpxA_peri. 1 hit.
PF00672. HAMP. 1 hit.
PF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM00304. HAMP. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
[Graphical view]
SUPFAMiSSF47384. SSF47384. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEiPS50885. HAMP. 1 hit.
PS50109. HIS_KIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Cpx proteins of Escherichia coli K12. Immunologic detection of the chromosomal cpxA gene product."
    Albin R., Weber R.F., Silverman P.M.
    J. Biol. Chem. 261:4698-4705(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TOPOLOGY.
    Strain: K12.
  2. "The cpx proteins of Escherichia coli K12. Structure of the cpxA polypeptide as an inner membrane component."
    Weber R.F., Silverman P.M.
    J. Mol. Biol. 203:467-478(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
    Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "The Cpx proteins of Escherichia coli K-12: evidence that cpxA, ecfB, ssd, and eup mutations all identify the same gene."
    Rainwater S., Silverman P.M.
    J. Bacteriol. 172:2456-2461(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, DISRUPTION PHENOTYPE.
    Strain: K12 / AE2000.
  7. "Accumulation of the F plasmid TraJ protein in cpx mutants of Escherichia coli."
    Silverman P.M., Tran L., Harris R., Gaudin H.M.
    J. Bacteriol. 175:921-925(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: K12.
  8. "The Cpx two-component signal transduction pathway of Escherichia coli regulates transcription of the gene specifying the stress-inducible periplasmic protease, DegP."
    Danese P.N., Snyder W.B., Cosma C.L., Davis L.J., Silhavy T.J.
    Genes Dev. 9:387-398(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, DISRUPTION PHENOTYPE.
    Strain: K12 / MC4100.
  9. "The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems."
    Jones C.H., Danese P.N., Pinkner J.S., Silhavy T.J., Hultgren S.J.
    EMBO J. 16:6394-6406(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  10. "Transduction of envelope stress in Escherichia coli by the Cpx two-component system."
    Raivio T.L., Silhavy T.J.
    J. Bacteriol. 179:7724-7733(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A KINASE AND PHOSPHATASE, CATALYTIC ACTIVITY, COFACTOR, DOMAIN, AUTOPHOSPHORYLATION, MUTAGENESIS OF ARG-33; 93-ARG--GLY-124 AND THR-252.
    Strain: K12 / MC4100.
  11. "CpxP, a stress-combative member of the Cpx regulon."
    Danese P.N., Silhavy T.J.
    J. Bacteriol. 180:831-839(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, DISRUPTION PHENOTYPE.
    Strain: K12 / MC4100.
  12. "Tethering of CpxP to the inner membrane prevents spheroplast induction of the cpx envelope stress response."
    Raivio T.L., Laird M.W., Joly J.C., Silhavy T.J.
    Mol. Microbiol. 37:1186-1197(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, DISRUPTION PHENOTYPE.
    Strain: K12 / MC4100.
  13. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: K12 / MG1655 / ATCC 47076.
  14. "Cpx signal transduction is influenced by a conserved N-terminal domain in the novel inhibitor CpxP and the periplasmic protease DegP."
    Buelow D.R., Raivio T.L.
    J. Bacteriol. 187:6622-6630(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, PROBABLE SUBUNIT.
    Strain: K12 / MC4100.
  15. "Purification, reconstitution, and characterization of the CpxRAP envelope stress system of Escherichia coli."
    Fleischer R., Heermann R., Jung K., Hunke S.
    J. Biol. Chem. 282:8583-8593(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  16. "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia coli."
    Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J., Walker G.C.
    Mol. Cell 36:845-860(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN HYDROXYUREA RESISTANCE, DISRUPTION PHENOTYPE.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  17. Cited for: SUBUNIT.
    Strain: K12 / MC4100.
  18. "Structural basis for two-component system inhibition and pilus sensing by the auxiliary CpxP protein."
    Zhou X., Keller R., Volkmer R., Krauss N., Scheerer P., Hunke S.
    J. Biol. Chem. 286:9805-9814(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  19. "Dynamic interaction between the CpxA sensor kinase and the periplasmic accessory protein CpxP mediates signal recognition in E. coli."
    Tschauner K., Hoernschemeyer P., Mueller V.S., Hunke S.
    PLoS ONE 9:E107383-E107383(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH CPXP AND CPXR, SUBCELLULAR LOCATION.
    Strain: K12 / MG1655 / ATCC 47076.
  20. "Segmental helical motions and dynamical asymmetry modulate histidine kinase autophosphorylation."
    Mechaly A.E., Sassoon N., Betton J.M., Alzari P.M.
    PLoS Biol. 12:E1001776-E1001776(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 188-457 IN COMPLEX WITH ADP; ATP AND ATP ANALOG, FUNCTION, SUBUNIT, ACTIVE SITE, REACTION MECHANISM, DOMAIN, AUTOPHOSPHORYLATION, MUTAGENESIS OF SER-185; LEU-186; ALA-197; ASN-204; GLY-222; MET-228 AND ASN-356.

Entry informationi

Entry nameiCPXA_ECOLI
AccessioniPrimary (citable) accession number: P0AE82
Secondary accession number(s): P08336, Q2M8K8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: December 6, 2005
Last modified: July 6, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.