ID A0A0U3JW42_9BURK Unreviewed; 739 AA.
AC A0A0U3JW42;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Hrubri_3800 {ECO:0000313|EMBL:ALU90957.1};
OS Herbaspirillum rubrisubalbicans M1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=1078773 {ECO:0000313|EMBL:ALU90957.1, ECO:0000313|Proteomes:UP000069903};
RN [1] {ECO:0000313|EMBL:ALU90957.1, ECO:0000313|Proteomes:UP000069903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1 {ECO:0000313|EMBL:ALU90957.1,
RC ECO:0000313|Proteomes:UP000069903};
RA Balsanelli E., Cardoso R.L.A., Cruz L.M., Faoro H., Chubatsu L.S.,
RA Muller-Santos M., Baura V.A., Huergo L.F., Wassem R., Broughton W.,
RA Monteiro R.A., Souza E.M., Pedrosa F.O.;
RT "Herbaspirillum rubrisubalbicans M1 complete genome.";
RL Submitted (DEC-2015) 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; CP013737; ALU90957.1; -; Genomic_DNA.
DR RefSeq; WP_058896669.1; NZ_CP013737.1.
DR AlphaFoldDB; A0A0U3JW42; -.
DR STRING; 1078773.Hrubri_3800; -.
DR KEGG; hrb:Hrubri_3800; -.
DR OrthoDB; 9146932at2; -.
DR Proteomes; UP000069903; Chromosome.
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; 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; 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 PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ALU90957.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Transferase {ECO:0000313|EMBL:ALU90957.1}.
FT DOMAIN 149..261
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 357..591
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 593..730
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT COILED 290..324
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 200
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 739 AA; 79443 MW; DB3A87FB3208F9DD CRC64;
MKLDSASVID AATSAAAPDL PDAADTFAAD TVLRETLRPL LAIVRQQSAA WGARQESEDG
PRAAVPPLAL RSLAALRDYA RSSSAEPFAD AAARLFALLE QQSAQADLDP LTRSIIQADI
EQLAQLLEAP LTATAGAVAA GVPAAPAMHE EIDPLLLPVF LEEAQELITG IGETLLALPA
AEHRGVADAS LLAELARPLH TLKGSARMVG ARHLSRCLHD METTLQRLAL DDAVQESGSL
AALLALYDQA IEQFNTLEQG LAVSSSPARR DGLADSQLTA PLIRIRTTLL DKLLNQVGEV
SIRRAQLDNE ITALQGDARA LGEQLGKLAE QLGQLQRHCG DTPWVAPPGQ DPDSAAPLAL
AGSMQEALGE ALQHQKQLLQ RVLKTREDLR QQGRTTRELQ QELMHARMVK FNSMESRMQH
LARQVALETG KPLTLELSDY RLHIDRAILE RLMGPLEHLL RNAAVHGIED AEVRRAAGKP
VSGQLRIQAS HEGNEAVIRV SDDGRGLDLQ AIRDKARQRG LIEAQQISEA RLAELIFEPG
FSTSTQVSAL AGRGVGMDVV RAEVAALGGR MTVHSRAGRG VLFTLYLPLS LAVQHVCLLR
HGQQPYAIPS TLIERVVQLR SDQAQDALQQ RALEFNGQRL ALYPLHCLLD EPAHPAWPDP
SDSAFALLIK RGDELMVIMA DHVSGNREVV VKPVGPQVAT LAGVVGATVL GDGQIVLIIN
PLLLSGSRRA DGRAAEPAP
//
