ID   D1YZQ8_METPS            Unreviewed;       613 AA.
AC   D1YZQ8;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=MCP_1858 {ECO:0000313|EMBL:BAI61930.1};
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI61930.1, ECO:0000313|Proteomes:UP000001882};
RN   [1] {ECO:0000313|Proteomes:UP000001882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC   {ECO:0000313|Proteomes:UP000001882};
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(2011).
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; AP011532; BAI61930.1; -; Genomic_DNA.
DR   AlphaFoldDB; D1YZQ8; -.
DR   STRING; 304371.MCP_1858; -.
DR   KEGG; mpd:MCP_1858; -.
DR   eggNOG; arCOG02352; Archaea.
DR   eggNOG; arCOG06192; Archaea.
DR   eggNOG; arCOG06515; Archaea.
DR   InParanoid; D1YZQ8; -.
DR   Proteomes; UP000001882; Chromosome.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00130; PAS; 2.
DR   Gene3D; 2.10.70.100; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 3.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 3.
DR   PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF08447; PAS_3; 2.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00086; PAC; 3.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 2.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:BAI61930.1};
KW   Transferase {ECO:0000313|EMBL:BAI61930.1}.
FT   DOMAIN          11..81
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          136..205
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          209..259
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          334..385
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          396..612
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   613 AA;  70042 MW;  91D78C01F11582F8 CRC64;
     MEKLESILRS GEEMSRQFLE QTLYGVWVNV DSRTVFINKE GARILGAFHP RDIIGKSIFE
     FIHPDYHEVA KDRIRMIHET GDPMAIVQEK CIRLDGRAVD VDIWLMKFRY EGKPAIFAAF
     RDITERRQAE RALKESEEKF RALAESAKAG IILTRADKFI YVNPETIKDL GYTKDELLAM
     KFWDVVHPDS RELVRSQGLK LLQGLPAPST YEIKVLTKGG KTLWEELTAT IIDYIGEPTI
     LITSFNITER KRAEIALRES EYELNKAQRI AHLGSWEWDL ASNKVRGSDE LYRMFGLTPG
     LETPLDQFIE QVAPEDRQRL MNALGETVKY NKPFDMEYQV LLPDGTRRFI DDKAEVSYEG
     GRPATVFGTV LDITERKRVE NELKAAKMQA DLYVDLMSHD ISNMNQVGMG FLEMALDMLD
     LDEMGREMLL KPKSAFENSS KLIDNVKKLQ KARSGKYSER EMDIGQVLGK VRDNYSKQYG
     PNVTINYLMS SGYMVKANEL LYDLFSNLVE NAIKHAKAHP MIDINVEPAR ENGRVYYRVT
     IDDQGPGIPD ELKSVIFERK LTGDIKSKGS GIGLYMVKTL ADIYNGRVWV EDRVPGDRTK
     GARFVAMLPA VEK
//