ID A5G500_GEOUR Unreviewed; 558 AA.
AC A5G500;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Gura_2694 {ECO:0000313|EMBL:ABQ26868.1};
OS Geotalea uraniireducens (strain Rf4) (Geobacter uraniireducens).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geotalea.
OX NCBI_TaxID=351605 {ECO:0000313|EMBL:ABQ26868.1, ECO:0000313|Proteomes:UP000006695};
RN [1] {ECO:0000313|EMBL:ABQ26868.1, ECO:0000313|Proteomes:UP000006695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rf4 {ECO:0000313|EMBL:ABQ26868.1,
RC ECO:0000313|Proteomes:UP000006695};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Shelobolina E., Aklujkar M.,
RA Lovley D., Richardson P.;
RT "Complete sequence of Geobacter uraniireducens Rf4.";
RL Submitted (MAY-2007) 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; CP000698; ABQ26868.1; -; Genomic_DNA.
DR RefSeq; WP_011939544.1; NC_009483.1.
DR AlphaFoldDB; A5G500; -.
DR STRING; 351605.Gura_2694; -.
DR KEGG; gur:Gura_2694; -.
DR HOGENOM; CLU_000650_3_6_7; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000006695; 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; 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 Kinase {ECO:0000313|EMBL:ABQ26868.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000006695};
KW Transferase {ECO:0000313|EMBL:ABQ26868.1}.
FT DOMAIN 3..111
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 174..415
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 417..551
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT MOD_RES 54
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 558 AA; 60686 MW; A7EFA2906F5C1BE5 CRC64;
MDTTIDMSVL LDEFLEDAAE HLEAAESSLL LLEKRVNDGL HDEGGVTLLL GNLHTLKGNA
GMMGLTPLQQ YVHKMESVLK QVVDGSLSLT SNLFESFYSA INSLRESLEK LAKNSAEPLD
FSDELTLLEY LVSGGAERNG GISYGREKKD DFGYITQKSN TLKVNFEKLD DLLNLVGELV
IQRTTLLAFE AKLKETVKDR AVIEAFSESS QLIGKSAADL REAIMKVRML PVKVVFQRFN
RLVRDLSHKH GKEINLVFEG EETELDKTVV DEIGEPLLHL IRNAVDHGIE SPDERRMVGK
PPVATVALRA RHENNHMIVS VEDDGRGISI EKLKNSAVAK GLIDHQQARA LTDQEALQLV
FIPGFSTSRE VTETSGRGIG LDVVKNAVTA FNGMIDIDSM HGAGTTFTIK LPLTLAIIAS
LMVEVSGEVF AVPLSGVLES IKIDKAEIHQ VASGEIINLR DRILPIVRLN EFFGLNNTPT
TEEMEYVVIV GSGEKRGGII VDRLIGQQEI VIKAMDDYLG PLPGISGGTV LGDGSVALIL
DIGSLMGKTG RGGTDGGL
//
