ID   CPXA_ECOL6              Reviewed;         457 AA.
AC   P0AE83; P08336;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Sensor protein CpxA;
DE            EC=2.7.13.3;
GN   Name=cpxA; OrderedLocusNames=c4863;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: This protein is involved in several diverse cellular
CC       processes, such as the functioning of acetohydroxyacid synthetase I, in
CC       the biosynthesis of isoleucine and valine, the TraJ protein activation
CC       activity for tra gene expression in F plasmid, and the synthesis,
CC       translocation, or stability of cell envelope proteins. Activates CpxR
CC       by phosphorylation (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
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DR   EMBL; AE014075; AAN83291.1; -; Genomic_DNA.
DR   RefSeq; WP_000580417.1; NC_004431.1.
DR   AlphaFoldDB; P0AE83; -.
DR   SMR; P0AE83; -.
DR   STRING; 199310.c4863; -.
DR   EnsemblBacteria; AAN83291; AAN83291; c4863.
DR   GeneID; 66672180; -.
DR   KEGG; ecc:c4863; -.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_000445_89_27_6; -.
DR   OMA; ANDLLWW; -.
DR   BioCyc; ECOL199310:C4863-MON; -.
DR   BRENDA; 2.7.13.3; 2026.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 3.30.450.210; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR032404; CpxA_peri.
DR   InterPro; IPR038515; CpxA_peri_sf.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF16527; CpxA_peri; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..457
FT                   /note="Sensor protein CpxA"
FT                   /id="PRO_0000074741"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        8..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        30..163
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        185..457
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          185..237
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          245..455
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         248
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   457 AA;  51624 MW;  720EE4A62885BA33 CRC64;
     MIGSLTARIF AIFWLTLALV LMLVLMLPKL DSRQMTELLD SEQRQGLMIE QHVEAELAND
     PPNDLMWWRR LFRAIDKWAP PGQRLLLVTT EGRVIGAERS EMQIIRNFIG QADNADHPQK
     KKYGRVELVG PFSVRDGEDN YQLYLIRPAS SSQSDFINLL FDRPLLLLIV TMLVSTPLLL
     WLAWSLAKPA RKLKNAADEV AQGNLRQHPE LEAGPQEFLA AGASFNQMVT ALERMMTSQQ
     RLLSDISHEL RTPLTRLQLG TALLRRRSGE SKELERIETE AQRLDSMIND LLVMSRNQQK
     NALVSETIKA NQLWSEVLDN AAFEAEQMGK SLTVNFPPGP WPLYGNPNAL ESALENIVRN
     ALRYSHTKIE VGFAVDKDGI TITVDDDGPG VSPEDREQIF RPFYRTDEAR DRESGGTGLG
     LAIVETAIQQ HRGWVKAEDS PLGGLRLVIW LPLYKRS