ID B6BFS4_9RHOB Unreviewed; 391 AA.
AC B6BFS4;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 24-JAN-2024, entry version 57.
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:EDZ44805.1};
GN ORFNames=RBY4I_168 {ECO:0000313|EMBL:EDZ44805.1};
OS Rhodobacterales bacterium Y4I.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales.
OX NCBI_TaxID=439496 {ECO:0000313|EMBL:EDZ44805.1, ECO:0000313|Proteomes:UP000005133};
RN [1] {ECO:0000313|EMBL:EDZ44805.1, ECO:0000313|Proteomes:UP000005133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y4I {ECO:0000313|EMBL:EDZ44805.1,
RC ECO:0000313|Proteomes:UP000005133};
RA Moran M.A., Buchan A., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) 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};
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DR EMBL; DS995283; EDZ44805.1; -; Genomic_DNA.
DR AlphaFoldDB; B6BFS4; -.
DR STRING; 439496.RBY4I_168; -.
DR eggNOG; COG0643; Bacteria.
DR HOGENOM; CLU_000650_3_0_5; -.
DR Proteomes; UP000005133; 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 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; 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; IPR004358; Sig_transdc_His_kin-like_C.
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 PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000005133}.
FT DOMAIN 1..240
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 242..377
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
SQ SEQUENCE 391 AA; 41459 MW; 6465072D585B0012 CRC64;
MDRLINAVGE LIINHSMLAQ QIANLNVSDT RDVETELEGF KNLARDIQEG VMAIRAQPVK
PLFQRMARIV REASAATGKT CKLVTEGENT EVDKTVIERL SDPLTHILRN AVDHGVEKPE
DRAAAGKQTT GEIRLSASHR SGSVCIEIRD DGAGVNRPRV KQIAIEKGLI PENAELTDGE
IDNLLFAPGF STAKEISNLS GRGVGMDVVK NAVTGLGGRI NISSAPGKGS TFTIILPLTL
AVMDGMVVSV ADQTMVVPIT SIVETMRGSD DMINSLGADG TLLSIRGNFV PICDVAGALG
LYRESDRQAG VYLLVETETG QRCALAVDDI HDQRQVVIKS LDGVCGEIPG VAAATILGDG
KIAMILDPES IIAASPTAAA FDTERRLSNA S
//
