CPXA_ECO57
ID CPXA_ECO57 Reviewed; 457 AA.
AC P0AE84; P08336;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Sensor protein CpxA;
DE EC=2.7.13.3;
GN Name=cpxA; OrderedLocusNames=Z5456, ECs4837;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG59105.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38260.1; -; Genomic_DNA.
DR PIR; E91233; E91233.
DR RefSeq; NP_312864.1; NC_002695.1.
DR RefSeq; WP_000580417.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AE84; -.
DR SMR; P0AE84; -.
DR STRING; 155864.EDL933_5240; -.
DR PRIDE; P0AE84; -.
DR EnsemblBacteria; AAG59105; AAG59105; Z5456.
DR EnsemblBacteria; BAB38260; BAB38260; ECs_4837.
DR GeneID; 66672180; -.
DR GeneID; 914983; -.
DR KEGG; ece:Z5456; -.
DR KEGG; ecs:ECs_4837; -.
DR PATRIC; fig|386585.9.peg.5058; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_89_27_6; -.
DR OMA; ANDLLWW; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..457
FT /note="Sensor protein CpxA"
FT /id="PRO_0000074740"
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"
FT CONFLICT 237
FT /note="T -> S (in Ref. 1; AAG59105)"
FT /evidence="ECO:0000305"
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
