ID A0A1V4CCW3_9BURK Unreviewed; 689 AA.
AC A0A1V4CCW3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BC358_13890 {ECO:0000313|EMBL:OPF62469.1};
OS Hydrogenophaga sp. H7.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Hydrogenophaga.
OX NCBI_TaxID=1882399 {ECO:0000313|EMBL:OPF62469.1, ECO:0000313|Proteomes:UP000189907};
RN [1] {ECO:0000313|Proteomes:UP000189907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H7 {ECO:0000313|Proteomes:UP000189907};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPF62469.1}.
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DR EMBL; MCIC01000017; OPF62469.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4CCW3; -.
DR STRING; 1882399.BC358_13890; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000189907; Unassembled WGS sequence.
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; cd00731; CheA_reg; 1.
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:SF10; 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 Reference proteome {ECO:0000313|Proteomes:UP000189907}.
FT DOMAIN 13..117
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 344..552
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 554..689
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT MOD_RES 60
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 689 AA; 73886 MW; 46BDA47774ACDDDA CRC64;
MAEATHENSS AGGNIDLSQF YQIFFEEAGE NLDQMEQMLL ALDLEHADDE ELNAIFRCAH
SIKGGAATFG FADVAELTHQ MESLLDKLRR HELQPTPPMV DVLLESSDAL KLLLARHQGQ
GVEPPPTGEL VARISALAHG TAVAVPAPAP VAAAAAPVQA PTPAPAAALA EGERKLTIRI
GPLDQLAQAD GIGELFRDIA GLGRIESTRD DGQFRSLEVF TRSSDSDLLD LFTFHVSKEQ
IQISEAGAPT TGEGRDFGFF DDAPGTPAAP AAVAPAVPVA QAAPAAKPAP RAEARPAAAG
GLESSTLRVS VSKVDQLINL VGELVITQAM LAQKSRELDS TANQQLLAGL VDLDRNTRDL
QEAVMSIRMI PMSVVFNRFP RMLRDLASKL GKKVELITHG EATELDKGLI EKITDPLTHL
IRNSCDHGIE MPEERLARGK PDHGTITLSA SHQGGSILIE VRDDGKGLSR EKLLRKAREK
GMDAPDTMTD TEVWNLIMAP GFSTAEVVTD VSGRGVGMDV VKKNILSLGG TVEIDSAEGY
GMSVKVRLPL TLAIMDGMSV RVSDEVYILP LSSVIESFQI NPGDINTVAQ GAQLVKVREE
YMPVIELEKI FSVPRFEFHG GSPIMVVVEA EGSRVALMVD ELLGQQQVVI KNLESNYRKV
PNVSGATILG DGKVALILDT SGLVRRSRH
//
