ID Q2FLJ4_METHJ Unreviewed; 890 AA.
AC Q2FLJ4;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Mhun_0640 {ECO:0000313|EMBL:ABD40396.1};
OS Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS JF-1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX NCBI_TaxID=323259 {ECO:0000313|EMBL:ABD40396.1, ECO:0000313|Proteomes:UP000001941};
RN [1] {ECO:0000313|Proteomes:UP000001941}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1
RC {ECO:0000313|Proteomes:UP000001941};
RX PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL Stand. Genomic Sci. 11:2-2(2016).
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; CP000254; ABD40396.1; -; Genomic_DNA.
DR RefSeq; WP_011447680.1; NC_007796.1.
DR AlphaFoldDB; Q2FLJ4; -.
DR STRING; 323259.Mhun_0640; -.
DR EnsemblBacteria; ABD40396; ABD40396; Mhun_0640.
DR GeneID; 25393450; -.
DR KEGG; mhu:Mhun_0640; -.
DR eggNOG; arCOG02320; Archaea.
DR eggNOG; arCOG06193; Archaea.
DR HOGENOM; CLU_324325_0_0_2; -.
DR InParanoid; Q2FLJ4; -.
DR OrthoDB; 110779at2157; -.
DR Proteomes; UP000001941; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd12912; PDC2_MCP_like; 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; 3.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR45528; SENSOR HISTIDINE KINASE CPXA; 1.
DR PANTHER; PTHR45528:SF9; SENSOR HISTIDINE KINASE YRKQ; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
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); 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:ABD40396.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001941};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABD40396.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 296..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 320..373
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 392..466
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 626..678
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 787..886
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 519..563
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 662..689
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 890 AA; 102174 MW; 67D3FB03884E1F10 CRC64;
MTYPTSPHTI PYLQRITTRT ILSIVLLVIL MVMIVGCGVI WIAYSEQGNT IHLTQKKTAE
EVSLIISYYF SNLADNLMLL STSSHFSTLS IKEQKEVLID LLNDKRKLYH ECTVLTPDGK
EVLKLSRFYT YMPDELGNRS TESLFNRALK GETVISPIYV FPQTGLISVD IAIPVSDHQG
AITHVLIGTA SVLPLWSEIE KIDLGNSGYV YIVDKEGKFV AYQKISDILD RYGSLMTAYP
PVQDVISEKS ERTNISPYIG LKGEEVIGSY ADIEGTDWAV IIELSTTEAF ENILRMIHVT
IAALIIGALF SGLLGYVLSR YLTDPVLNLT FTVSKIGQGN LVTDIHEITR TDEIGILARG
IEQMQKNLRE SYLDLELRIS ELTLAREKLR ISEEQYRTIF EHSENPLILV EKDFSISLIN
KKFEELWGYS QDEVIGQKKW VEFVADPEER NRMIEYNKRR QAGEKDIPSL YNFRFKTRYG
EIRDIMISVT QMPGTGQTLA TLVDVTEQKR FEQELIQKNS DLHEAYEKLA ANEEELRESY
NTLATFEQEL RMSEQKYRNI VEDQTELILR FTPQRKIIFV NDAFCSFFQL NREDILQQGG
EIQEIEEYLS GILNQITALS SDNPVAFFEC RIFQPDGEER WINGTIRGLF DDSGSITEYQ
SVARDISDRK KAEEALEKAR NKLTLLNAIT FEDIRNYIFT LSGYLEVQKD MVSDPAVLTL
FEKEKSIVKK VSQSLEFAKD YQDMGIKPAY WQNVLQVYLY AISHLDLTHI ERVEEIKGVF
MYADPLLEKV FFNLAMNLVI HGKNTVTRLH LYTEMQGNDL KIIFEDNGQG IPDEQKETLF
QRRNDLKKGM GLYFVREVLA ITGIRIQETG VFGQGARFEL IVPYGKYRFE
//
