ID F8AK23_METOI Unreviewed; 954 AA.
AC F8AK23;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Metok_1419 {ECO:0000313|EMBL:AEH07384.1};
OS Methanothermococcus okinawensis (strain DSM 14208 / JCM 11175 / IH1).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanothermococcus.
OX NCBI_TaxID=647113 {ECO:0000313|EMBL:AEH07384.1, ECO:0000313|Proteomes:UP000009296};
RN [1] {ECO:0000313|EMBL:AEH07384.1, ECO:0000313|Proteomes:UP000009296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14208 / JCM 11175 / IH1
RC {ECO:0000313|Proteomes:UP000009296};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Held B., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Sieprawska-Lupa M., Takai K.,
RA Miyazaki J., Whitman W., Woyke T.;
RT "Complete sequence of chromosome of Methanothermococcus okinawensis IH1.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEH07384.1, ECO:0000313|Proteomes:UP000009296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14208 / JCM 11175 / IH1
RC {ECO:0000313|Proteomes:UP000009296};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Held B., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Sieprawska-Lupa M., Takai K.,
RA Miyazaki J., Whitman W., Woyke T.;
RT "Complete sequence of chromosome of Methanothermococcus okinawensis IH1.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; CP002792; AEH07384.1; -; Genomic_DNA.
DR RefSeq; WP_013867566.1; NC_015636.1.
DR AlphaFoldDB; F8AK23; -.
DR STRING; 647113.Metok_1419; -.
DR GeneID; 10773576; -.
DR KEGG; mok:Metok_1419; -.
DR eggNOG; arCOG04403; Archaea.
DR HOGENOM; CLU_000650_3_2_2; -.
DR OrthoDB; 293137at2157; -.
DR Proteomes; UP000009296; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
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; 3.30.70.1110; Histidine kinase CheA-like, P2 response regulator-binding domain; 2.
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; IPR037052; CheA-like_P2_sf.
DR InterPro; IPR010808; CheA_P2-bd.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR035891; CheY-binding_CheA.
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 Pfam; PF07194; P2; 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; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF55052; CheY-binding domain of CheA; 2.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000313|EMBL:AEH07384.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Transferase {ECO:0000313|EMBL:AEH07384.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..104
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 575..825
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 827..954
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 540..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 954 AA; 107334 MW; EFD3D77FF7258A2D CRC64;
MDEMEQYKEL FMAEATEHLE ALNQNLVELE NNPDNKDIIN LIFRSAHTLK GSARTLGFDN
ISNLTHHMED ILDNIRNGEI AVNSEIMDLL FKCLDALETM VNEIEEDAET SSIDVDSIVN
EIKTLKEKYM GNGGSSASEA SKSNVNISKV AENEESKKEN NNTQNTKSTI SIVLKEPKTT
VNIKTNLNDE KNEGNENEIK KPKNLDEILS QMSKSVEVLN IVADAFNYDD LKETLTKIND
LVNYVLNEDI IFNKSVMEAL KCSLDAMEKI AKSFEENGGI DNLDIDLSKI NKKIDDAITL
KHEHRSSSDN VKEYGVILDH SKFDFNKYAE HIKEMVDNGY TLYHLKSKVL EDCDLKSVRL
SMVISNIKKI GDILISTPSE EEIKEKSHDE LEIIFLSNKQ LDEITKVFDT MCEMEYIAVA
PINIDFKIGN IGGVDEGGNN NETVKDDRIK DAYKLKIIID EECILKSVRA YMAIKELKNV
GEIIKTEPSC EKLQEGEFDG NEVVVYIISN KEEDDLKEIV FSIPEIKNVI IETPEYLKEQ
SKMKKNSKPH EKSSTSTKPQ NSKKKPSEKS GEKKTLTQTV RINIEKLDKL MNLVGELVIN
RANFTQIANK YNIKELHNAV NRLNMLATEL QEEVMAMRMI PVSFIFNRFP RTVRDTSKAL
NKEVELIIEG SDIELDRTVL DELAEPLTHI IRNSLDHGIE TPEEREKKGK PRKGTLKLVA
TRERNHVLIT IEDDGKGIDP EIIKKKAVEK GIISEDDANK LSDQEAINLV FLPGFSTAEK
VSDVSGRGVG MDVVKSKIES LGGSVSLYSE KEKGTKIILQ LPLTMAIILA LLIKLRDQVY
AIPLTSVLDV THVKKEDISN LEGQDAIIYR NHILPVIWLR DILNDYSAEE SEDVYIIVIE
RNSGKLGVVV DDVIGREEIV VKPLTGILKN IHGLAGATIL GDGRVALILD LNNI
//
