ID D1YYD8_METPS Unreviewed; 725 AA.
AC D1YYD8;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=MCP_1388 {ECO:0000313|EMBL:BAI61460.1};
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:BAI61460.1, 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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; AP011532; BAI61460.1; -; Genomic_DNA.
DR AlphaFoldDB; D1YYD8; -.
DR STRING; 304371.MCP_1388; -.
DR KEGG; mpd:MCP_1388; -.
DR eggNOG; arCOG02352; Archaea.
DR eggNOG; arCOG04446; Archaea.
DR eggNOG; arCOG06515; Archaea.
DR InParanoid; D1YYD8; -.
DR OrthoDB; 3369at2157; -.
DR Proteomes; UP000001882; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd12914; PDC1_DGC_like; 1.
DR CDD; cd12912; PDC2_MCP_like; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 6.10.340.10; -; 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; IPR033479; dCache_1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
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; IPR029151; Sensor-like_sf.
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; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08447; PAS_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF103190; Sensory domain-like; 2.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAI61460.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 302..355
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 395..439
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 442..495
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 506..724
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 479..506
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 725 AA; 80426 MW; 20E776E59929155B CRC64;
MASIKVKVIV LVLLMILPII LIGAAGTLYF QYTIRQTIWD DNLAQAKAIS AMTPEYMGAS
QLYLTSIADR PLVVRAMENG DTAFLTSMAA YANSTERINS VYFTDKNGTV LAATAPLSGL
IGTSAVDRPY VNNVTMTGMP YIGDTEPGID RTPVVAIGVP VKNNNGTVIG VMVGTIDLDD
YAKTVLGTQV KNQQYIYLVN RTGHIIVHNN PQYVLEMRDY TSVPAVQRVL NGETGVMENH
NPVENDDRLA AYTPIKTLGW GVIVAIPVNV AYEPVRNATT WMVAIVATTV ILSMILGLYV
GNGITSPITK LSTAVKMAGE SENYRHMLPL GRDDEIGELA RSFSGMMDII KKDIEELKRT
GDALRKGQHI LTKSQEVAHV GNWAWNVQTG ELTGSPECDR IFGYEPGQVR PSHNWAISRV
HPDDRKIMEG LMETAIRTGK RGGADYRIVR PDGTIRYVNT IVDKIVHDKA GKVKWLYGIS
QDITERKQAE ESMKEAKQRA ELYLDLMGHD INNINQVAMG YLELANDRLP LSEEEKELIS
TPLDALKSSA RLIENVRKLQ RSKEGDLKTE VIDMGDVLSD VRDDYLRTSS DSIVIRYEKK
ESCHVLANSL IRDVFGNLIG NAIKHSEGRK PVEIDIRQDT MVENGKDYCR VAIEDNGPGI
PDQLKQKLFH RFQRGDTHAH GKGLGLYLVR TLVEDYHGRA WVEDRVPGDH TKGSRFVVIL
PLAGN
//
