ID J2Y0G3_9PSED Unreviewed; 612 AA.
AC J2Y0G3;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PMI38_03463 {ECO:0000313|EMBL:EJN37057.1};
OS Pseudomonas sp. GM84.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144340 {ECO:0000313|EMBL:EJN37057.1, ECO:0000313|Proteomes:UP000007504};
RN [1] {ECO:0000313|EMBL:EJN37057.1, ECO:0000313|Proteomes:UP000007504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM84 {ECO:0000313|EMBL:EJN37057.1,
RC ECO:0000313|Proteomes:UP000007504};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJN37057.1}.
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DR EMBL; AKJC01000201; EJN37057.1; -; Genomic_DNA.
DR AlphaFoldDB; J2Y0G3; -.
DR PATRIC; fig|1144340.3.peg.3295; -.
DR Proteomes; UP000007504; 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: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 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 Kinase {ECO:0000313|EMBL:EJN37057.1};
KW Transferase {ECO:0000313|EMBL:EJN37057.1}.
FT DOMAIN 264..473
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 475..609
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 201..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 612 AA; 64922 MW; 0E82D1B77DB03BE6 CRC64;
MAEPAGAEAP AAVAAPVVEA PVAEVDITDS EFEQLLDSLD AVKAEAEAAA EQLQGEALSG
SGDEITDAEF ESLLDQLHGK GQFSPEVAAA EPQVATASAP VSDEITDEEF ESLLDQLHGK
GTFQADALPG VAPVASETPT SSDEISDHEF EALLDQLHGK GKFSGDSVAA EAPAALAAPV
AAKAESQPVA KPAPAPAVPA AAAKPAAAPR PAAPAAEKHA VSEAETTVRV DTARLDEIMN
MVGELVLVRN RLVRLGLNSG DEAMSKAVSN LDVVTADLQT AVMKTRMQPI KKVFGRFPRL
VRDLARQLKK EINLELVGEE TDLDKNLVEA LADPLVHLVR NAVDHGVEMP DEREAAGKAR
TGRVVLSAEQ EGDHILLSIS DDGKGMDPNI LRAKAVEKGL MDKDAAERLS ESDCYNLIFA
PGFSTKTEIS DVSGRGVGMD VVKTKIAQLN GSINIFSAKG QGSKIVIKVP LTLAIMPTLM
VMLGNQAFAF PLVNVNEIFH LDLSRTNVVD GQEVVIVRDK ALPLFYLKRW LVQGQVHEEQ
REGHVVILSV GTQRIGFVVD QLVGQEEVVI KPLGKMLQGT PGMSGATITG DGRIALILDV
PSMLKRYAAR RI
//
