ID C3LM92_VIBCM Unreviewed; 761 AA.
AC C3LM92;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE AltName: Full=Phosphorelay protein LuxU {ECO:0000256|ARBA:ARBA00017260};
GN Name=cheA-1 {ECO:0000313|EMBL:ACP05668.1};
GN OrderedLocusNames=VCM66_1352 {ECO:0000313|EMBL:ACP05668.1};
OS Vibrio cholerae serotype O1 (strain M66-2).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=579112 {ECO:0000313|EMBL:ACP05668.1, ECO:0000313|Proteomes:UP000001217};
RN [1] {ECO:0000313|EMBL:ACP05668.1, ECO:0000313|Proteomes:UP000001217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M66-2 {ECO:0000313|EMBL:ACP05668.1,
RC ECO:0000313|Proteomes:UP000001217};
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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DR EMBL; CP001233; ACP05668.1; -; Genomic_DNA.
DR AlphaFoldDB; C3LM92; -.
DR SMR; C3LM92; -.
DR KEGG; vcm:VCM66_1352; -.
DR HOGENOM; CLU_000650_3_6_6; -.
DR Proteomes; UP000001217; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 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; 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:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 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; 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 Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..102
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 380..625
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 627..761
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT MOD_RES 44
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 761 AA; 85158 MW; 0019D8926051A77F CRC64;
MNPIMQNFII ESRDLIESAA RGLLALEANP DDKAIINELF REIHTVKGAS GILDNIAPFT
QLAHRMEDLM QKVRDGHVAL NGTMLDLMLG CCDQFLLWIE ELEQHQELSA EAVSISKQMI
AQLAPLTQAA PTHTPTPAVA AQEETATLSI SELTELLGRD CFNDVEALLE HPDALLLIYT
PDKQCFFSGD DPLAWMRSVE KVSWRKVVLI PDSEPFDTYQ AQMQFLLLTQ SAKKDLEQQL
APIEGQYRLY RIQSDNLPTA PIDQRTQYVE RIVKQQIALL REEQVSESVR AGTFLSIKNL
YCALSQQISD RPAPLPESVS ADELITLFDN ILLSFAHRTA IIDKCENEPA QPSAITVNEQ
LDKVKKKQIK TLKVDQEKVD LLMDLVGELI VAKNSMQYLA YRAENEFGVR KLAQDIKAEQ
SVISRLAEDL QSVVMQVRMV PLATVFQRYP RLIRDISRKL GKQVDLIIEG EDTEADKSIV
EDLSEPLVHL IRNALDHGIE SPDIRREQGK NPTGKITLSA FTLDDSVIIK MSDDGKGVDV
ERVKTKALER GLVEASKLER MSQQEIIHLI FEPGFSTVEQ VSDLSGRGVG MDAVRTAIER
NGGTLTLSSE PGKGSEITMI LPLSMTISRV MMFELEQQSF AIPIESVIQT LKISRHKDIR
RVKNLDTFIL RGETVPILYL KRAFEMNSAQ IYPDIQPILV VRVGDDVLGL AVDRLQEGQD
VIIKPLEGAL ATFSIYRGAA IMGDGRVLLV LDTEEVVKHA R
//
