ID A0A1M3M4X7_9PROT Unreviewed; 708 AA.
AC A0A1M3M4X7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BGO92_09035 {ECO:0000313|EMBL:OJX81192.1};
OS Magnetospirillum sp. 64-120.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=1895778 {ECO:0000313|EMBL:OJX81192.1, ECO:0000313|Proteomes:UP000184435};
RN [1] {ECO:0000313|EMBL:OJX81192.1, ECO:0000313|Proteomes:UP000184435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=64-120 {ECO:0000313|EMBL:OJX81192.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-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:OJX81192.1}.
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DR EMBL; MKVK01000011; OJX81192.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3M4X7; -.
DR STRING; 1895778.BGO92_09035; -.
DR Proteomes; UP000184435; 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}.
FT DOMAIN 5..109
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 357..565
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 567..703
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT MOD_RES 52
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 708 AA; 75713 MW; FA1DB461A5F4C0F2 CRC64;
MTDDQGYDLS QFKATYFEEC AELLATAEET IARLQEGQGN DEDLNAVFRC VHSIKGGAGA
FAFDELVHFA HVFETALDHL RSGRTELTPN VADLMVRGND ILGDFVRAAQ AETALPSDHG
ADILAQLAAL TGAKPPVAAQ TAPNAPKVES VKAPVFTTFR IRFLPGPDML RTGNDPLLMF
RELAGLGELE VKPDLGTLPS LTEMDALRSY VSWTCTLTTD KPRSAIDEVF EFVAGETAQV
EIEEVDSLPG DEEGEGWGLF APLPSTAAAR DEEGDGWGLF ADAPGSAVAT APVPMAPPKA
TAAAQQTAAQ GGAVHTASIR VDLDKIDRLV NMVGELVITQ AMLGQQASGF TVESHPELIQ
GLQELSHHTR ELQESVMAIR AQPVKALFSK APRLVRDLSS KLNKQARLVM SGENTEVDKT
VIEQLSDPLT HLIRNALDHG IETPEERMAV GKPAEGTIHL AAEHRSGRIF IEIQDDGRGI
HRERVLAKAM EKGLVEPGQQ LTDEQIDMLI FAPGFSTASE VSDVSGRGVG MDVVRKNIQD
VGGRVVVQSI PGAGSRFILS LPLTLAVMDG MLVQVGGQRY VLPLTNIVES LRPTPQQARS
LVDVGDVLTI RGEYINLMAL HAIFGIPGAI TDPTKGLVVI VETEGGERVG LLVDELLGQQ
QVVIKSLDSN FRPVHGISAA TILGDGRVAL ILDVSALRQM GALATAAQ
//
