ID C3T5E3_ECOLX Unreviewed; 654 AA.
AC C3T5E3;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=cheA {ECO:0000313|EMBL:EFC5412237.1};
GN ORFNames=BF481_000311 {ECO:0000313|EMBL:EFI1480002.1}, C9E67_11750
GN {ECO:0000313|EMBL:QCL47792.1}, CQ986_002861
GN {ECO:0000313|EMBL:EFC5412237.1}, ECs2598
GN {ECO:0000313|EMBL:ACI81927.1}, HVW43_01530
GN {ECO:0000313|EMBL:QMO39048.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:ACI81927.1};
RN [1] {ECO:0000313|EMBL:ACI81927.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=86-24 {ECO:0000313|EMBL:ACI81927.1}, 87-14
RC {ECO:0000313|EMBL:ACI81928.1}, TB182A {ECO:0000313|EMBL:ACI81929.1},
RC and TW14359 {ECO:0000313|EMBL:ACI81930.1};
RX PubMed=19439656; DOI=10.1073/pnas.0812949106;
RA Leopold S.R., Magrini V., Holt N.J., Shaikh N., Mardis E.R., Cagno J.,
RA Ogura Y., Iguchi A., Hayashi T., Mellmann A., Karch H., Besser T.E.,
RA Sawyer S.A., Whittam T.S., Tarr P.I.;
RT "A precise reconstruction of the emergence and constrained radiations of
RT Escherichia coli O157 portrayed by backbone concatenomic analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8713-8718(2009).
RN [2] {ECO:0000313|EMBL:QCL47792.1, ECO:0000313|Proteomes:UP000298553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=143 {ECO:0000313|EMBL:QCL47792.1,
RC ECO:0000313|Proteomes:UP000298553};
RA Bono J.L., Arthur T.M.;
RT "WGA of Escherichia coli O157:H7: comparison of multiple isolates.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000539823, ECO:0000313|Proteomes:UP000585348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MOD1-EC3652 {ECO:0000313|EMBL:EFI1480002.1,
RC ECO:0000313|Proteomes:UP000585348}, and MOD1-EC4555
RC {ECO:0000313|EMBL:EFC5412237.1, ECO:0000313|Proteomes:UP000539823};
RG GenomeTrakr network: Whole genome sequencing for foodborne pathogen traceback;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:QMO39048.1, ECO:0000313|Proteomes:UP000514754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHB10-C12 {ECO:0000313|EMBL:QMO39048.1,
RC ECO:0000313|Proteomes:UP000514754};
RA Shaw L.P.;
RT "REHAB project genomes.";
RL Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the transmission of sensory signals from the
CC chemoreceptors to the flagellar motors. CheA is autophosphorylated; it
CC can transfer its phosphate group to either CheB or CheY.
CC {ECO:0000256|ARBA:ARBA00035100}.
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: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; EU899376; ACI81927.1; -; Genomic_DNA.
DR EMBL; EU899377; ACI81928.1; -; Genomic_DNA.
DR EMBL; EU899378; ACI81929.1; -; Genomic_DNA.
DR EMBL; EU899379; ACI81930.1; -; Genomic_DNA.
DR EMBL; AASHWA010000013; EFC5412237.1; -; Genomic_DNA.
DR EMBL; AASYAS010000001; EFI1480002.1; -; Genomic_DNA.
DR EMBL; CP028607; QCL47792.1; -; Genomic_DNA.
DR EMBL; CP057906; QMO39048.1; -; Genomic_DNA.
DR RefSeq; WP_001322280.1; NZ_WTUQ01000004.1.
DR OMA; HSGNHVF; -.
DR Proteomes; UP000298553; Chromosome.
DR Proteomes; UP000514754; Chromosome.
DR Proteomes; UP000539823; Unassembled WGS sequence.
DR Proteomes; UP000585348; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; 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 GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR CDD; cd00731; CheA_reg; 1.
DR CDD; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 3.30.70.400; CheY-binding domain of CheA; 1.
DR Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR037006; CheA-like_homodim_sf.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR015162; CheY-binding.
DR InterPro; IPR035891; CheY-binding_CheA.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR PANTHER; PTHR43395:SF10; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF09078; CheY-binding; 1.
DR Pfam; PF02895; H-kinase_dim; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF55052; CheY-binding domain of CheA; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000313|EMBL:ACI81927.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00110}; Transferase {ECO:0000313|EMBL:ACI81927.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..105
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 302..509
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 511..646
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT MOD_RES 48
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 654 AA; 71412 MW; FF059676B523889B CRC64;
MSMDISDFYQ TFFDEADELL ADMEQHLLVL QPEAPDAEQL NAIFRAAHSI KGGAGTFGFS
VLQETTHLME NLLDEARRGE MQLNTDIINL FLETKDIMQE QLDAYKQSQE PDAASFDYIC
QALRQLALEA KGETPSAVTR LSVVAKSEPQ DEQSRSQLPR RIILSRLKAS EVDLLEEELG
HLTTLTDVVK GADSLSAILP GDIAEDDITA VLCFVIEADQ ITFETVEVSP KISTPPVLKL
AAEQAPTGRV EREKTTRSSE STSIRVAVEK VDQLINLVGE LVITQSMLAQ RSSELDPVNH
GDLITSMGQL QRNARDLQES VMSIRMMPME YVFSRYPRLV RDLAGKLGKQ VELTLVGSST
ELDKSLIERI IDPLTHLVRN SLDHGIELPE KRLAAGKNSV GNLILSAEHQ GGNICIEVTD
DGAGLNRERI LAKAASQGLT VSENMSDDEV AMLIFAPGFS TAEQVTDVSG RGVGMDVVKR
NIQEMGGHVE IQSKQGTGTT IRILLPLTLA ILDGMSVRVA DEVFILPLNA VMESLQPREA
DLHPLAGGER VLEVRGEYLP IVELWKVFNV AGAKTEATQG IVVILQSGGR RYALLVDQLI
GQHQVVVKNL ESNYRKVPGI SAATILGDGS VALIVDVSAL QAINREQRMA NTAA
//
