ID   D1Z2D4_METPS            Unreviewed;       643 AA.
AC   D1Z2D4;
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_2784 {ECO:0000313|EMBL:BAI62856.1};
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:BAI62856.1, 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; BAI62856.1; -; Genomic_DNA.
DR   AlphaFoldDB; D1Z2D4; -.
DR   STRING; 304371.MCP_2784; -.
DR   KEGG; mpd:MCP_2784; -.
DR   eggNOG; arCOG06192; Archaea.
DR   eggNOG; arCOG06516; Archaea.
DR   eggNOG; arCOG06712; Archaea.
DR   InParanoid; D1Z2D4; -.
DR   OrthoDB; 3369at2157; -.
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; 3.
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; IPR013656; PAS_4.
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; PF08448; PAS_4; 1.
DR   Pfam; PF13426; PAS_9; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 3.
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; 3.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:BAI62856.1};
KW   Transferase {ECO:0000313|EMBL:BAI62856.1}.
FT   DOMAIN          26..64
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          159..204
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          232..283
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          295..355
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          368..418
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          429..643
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   643 AA;  72000 MW;  8D008898EAD32067 CRC64;
     MVGMLPEDKG NFYDRLHDSV ILPSSIVEFY PDATLVVDNG GRVVAWNKAM GEMTGVPAED
     MLGKGNYEYS IPFYGKRMPI LVDMVGLPRE EVSSRYTNII VHGDTLEALT IKAKVKGRDV
     VLWGTAARLY GLNGKPVGAI ESIRDVTAQD MVERKLMESE EKYRTIITST NDAIITVDTK
     GIITYVNPSG IKMMGRPYDD IIGRHFTYFV VDAYKDRAIQ AFSQGMVGSP VPPLEIEMVD
     GDGRQVPIEL SGGALHSGRV KVGAIVTFRD VSERWKAHER LERRVKERTE ELALSEEKFR
     VLAETTSSAI FIYQKGRFRY VNPATCRITG YSEEELLTMN FWDWVHPDYQ ELVKRNGRAR
     RHGQLSPPRY EIKFVTRGGE ERWAELTPGL IEYNKRPAIL VTAVDITDRK RTEEALKNSK
     ENAEMYLDLM GHDINNMDQV ALGYLEMAMK AVQEDDPVYA YISRSYAMLQ ESSRLIDNLR
     KVQQAVDRKL RLEAVDLGAI LSEVAEEYSI VPGRDVTIEY RPVECQVMAS RLLKDVFSNI
     VGNAVKHSTG PLKVSIGVRP CVHNGVRCCE VSVEDDGPGI PEGLKDAIFS RMKRGSTKAP
     GSGLGLYIVR SLVEGFNGRV WAEDRVPGKP GDGSRFVVQL PSV
//