ID D1YYG3_METPS Unreviewed; 545 AA.
AC D1YYG3;
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_1413 {ECO:0000313|EMBL:BAI61485.1};
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:BAI61485.1, 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; BAI61485.1; -; Genomic_DNA.
DR AlphaFoldDB; D1YYG3; -.
DR STRING; 304371.MCP_1413; -.
DR KEGG; mpd:MCP_1413; -.
DR eggNOG; arCOG02353; Archaea.
DR eggNOG; arCOG06192; Archaea.
DR eggNOG; arCOG06515; Archaea.
DR InParanoid; D1YYG3; -.
DR OrthoDB; 8127at2157; -.
DR Proteomes; UP000001882; Chromosome.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
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; PF00989; PAS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
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); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:BAI61485.1};
KW Transferase {ECO:0000313|EMBL:BAI61485.1}.
FT DOMAIN 190..256
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 264..314
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 325..545
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 173..200
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 545 AA; 62294 MW; DB9B7A8AB990501A CRC64;
MRGILIHTDI KIGDRPETFY HSILDSLTSN IAILNDSGII IDINDSWDRF ALQNGIKSLD
KVGVGVSYFE VCRKAHGEHS DEAPVALDGL LSVLKGNISY FELEYPCDSP DKKRWFLMRA
TRFMENSRKY LVVTHIDITR RKMAETELLA SYKELETRYK AQAEISKDYG DMCKESIIEK
KRLEEALRKS EKKFQNLLER APFAIYIYRG EKNCCYVNPA AEALTGYTRD EFINMSYWDI
AHPDYRELVK ERGIKRQKGV TVPARYQIKI ITKSGDGRWI DINAANIMFE RKPAVLVTMI
DITEQKLAEE TLSEARAQAE VYIDLMSHDI NNMNQIAMGS LELFLDRSQT GKKIEGEDLK
LLRSSYLTLQ SISRLIDNVR KIQSLKSGMI RPEVVDTGLM IAEVIKAYEN IPGRDVKIHY
TPVFGYMVKA CELFQDVIVN IIDNAIKHST GPLLINIEDA EVIEDGKKYY RIFIEDNGPG
IPDEKKKDIF ERYKRGDTKA RGRGLGLYLV KTLIDDFGGK VWAEDRVPGE YGKGSKFVIM
LPAIT
//