ID Q1R407_ECOUT Unreviewed; 457 AA.
AC Q1R407;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=cpxA {ECO:0000313|EMBL:ABE09907.1};
GN OrderedLocusNames=UTI89_C4495 {ECO:0000313|EMBL:ABE09907.1};
OS Escherichia coli (strain UTI89 / UPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=364106 {ECO:0000313|EMBL:ABE09907.1, ECO:0000313|Proteomes:UP000001952};
RN [1] {ECO:0000313|EMBL:ABE09907.1, ECO:0000313|Proteomes:UP000001952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTI89 / UPEC {ECO:0000313|Proteomes:UP000001952};
RX PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA Chen S.L., Hung C.S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA Gordon J.I.;
RT "Identification of genes subject to positive selection in uropathogenic
RT strains of Escherichia coli: a comparative genomics approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}.
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DR EMBL; CP000243; ABE09907.1; -; Genomic_DNA.
DR RefSeq; WP_000580417.1; NZ_CP064825.1.
DR AlphaFoldDB; Q1R407; -.
DR SMR; Q1R407; -.
DR GeneID; 75204585; -.
DR KEGG; eci:UTI89_C4495; -.
DR HOGENOM; CLU_000445_89_27_6; -.
DR Proteomes; UP000001952; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16949; HATPase_CpxA-like; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.210; Two-component sensor protein CpxA, periplasmic domain; 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 PANTHER; PTHR45528; SENSOR HISTIDINE KINASE CPXA; 1.
DR PANTHER; PTHR45528:SF12; SENSOR HISTIDINE KINASE CPXA; 1.
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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABE09907.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABE09907.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 184..237
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 245..455
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
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
//
