ID A0A1G0YXM2_9BACT Unreviewed; 749 AA.
AC A0A1G0YXM2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A2X49_12385 {ECO:0000313|EMBL:OGV50591.1};
OS Lentisphaerae bacterium GWF2_52_8.
OC Bacteria; Lentisphaerota.
OX NCBI_TaxID=1798575 {ECO:0000313|EMBL:OGV50591.1, ECO:0000313|Proteomes:UP000179262};
RN [1] {ECO:0000313|EMBL:OGV50591.1, ECO:0000313|Proteomes:UP000179262}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGV50591.1}.
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DR EMBL; MHBJ01000134; OGV50591.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0YXM2; -.
DR Proteomes; UP000179262; 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; 2.
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; 2.
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; 2.
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; 2.
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; 2.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110}.
FT DOMAIN 2..110
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 178..284
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 347..598
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 600..735
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 308..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 227
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 749 AA; 81833 MW; 5362F6659B85192C CRC64;
MSRNDDLELI ESFVAESQDM IDTVEPMLLG LKDSGEGCAA DKEAINAVFR LFHSMKGAAG
FLKMENISAV THQAETLLDI FRHKDVPMDS SYIEVELEAI DAIRTMLELV TKTQSDKGME
SLRDTMTSSL KDALRRAELA AGMGAGKPAC PQGKEPECEK IVLDPVEEPQ SGQEILPELT
ITPEMAVRFS QEAAEILEQA EQGLLSIPHK TGEDKKATVS ETFRAIHSFK GNCGFMQLSD
LEHLSHKMEN VLDAMRSNKV DISEQNVDIL LKTLDVLRNG LCSFSRGEGG ELFNCELMME
FLEDLLPKEE SKDSQEPAAK LQEAPSPSET GLAGAELKAT GTGEIKTVRR DIRVDLEKLD
NLINLVGELV IAEAMVLRHP ALRTVDDETF DRAVHHLKRI SSNLQDVSMS VRMIPLSATF
RKMIRLVHDL SLKSGKKAGL ELIGEETEVD KNVIEQISDP LVHIIRNSLD HGLEAPAERS
AAEKPEKGIV TIAARHDGGE VVITVSDDGR GLNREKIIAK AVKQGLFNGD PSQLSDEEAY
QFIFEPGFST ADKVTDISGR GVGMDVVKKN IEKLNGRVTV KSNPGKGSDI SLHIPLTLAI
IDGMLVRVGS TQYTIPMLSI KESLKANTKQ ITVRPDGCEC VRLREELIPV LRLHHLYRKE
DAETELTKGI LVVVEADQEA AALLIDEIVG QQEIVIKGLS SYLGRPMGIS GCTVLGDGSV
SLIIDVGSLL RSAAESGFCD EEKAVGGEF
//
