ID Q2FLW9_METHJ Unreviewed; 974 AA.
AC Q2FLW9;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Mhun_1433 {ECO:0000313|EMBL:ABD41168.1};
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:ABD41168.1, 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};
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DR EMBL; CP000254; ABD41168.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2FLW9; -.
DR STRING; 323259.Mhun_1433; -.
DR EnsemblBacteria; ABD41168; ABD41168; Mhun_1433.
DR KEGG; mhu:Mhun_1433; -.
DR eggNOG; arCOG02343; Archaea.
DR eggNOG; arCOG06193; Archaea.
DR eggNOG; arCOG06538; Archaea.
DR HOGENOM; CLU_314417_0_0_2; -.
DR InParanoid; Q2FLW9; -.
DR OrthoDB; 8127at2157; -.
DR Proteomes; UP000001941; Chromosome.
DR GO; GO:0016020; C: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; cd00130; PAS; 2.
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; 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 InterPro; IPR013656; PAS_4.
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; PF02518; HATPase_c; 1.
DR Pfam; PF08448; PAS_4; 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; 3.
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); 3.
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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABD41168.1};
KW Membrane {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:ABD41168.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 298..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 322..374
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 619..661
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 705..757
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 768..963
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 974 AA; 111346 MW; 7DB85442DC37890E CRC64;
MILFIGIIFI SLISVTGYYY IETSKQIDER FRQNLIQTEL GLKSASDRIT KGQMLWEATY
KKPLLAVTNL VLKEYERSSR TPSEMNFDDI ITRIDPAYKD RIDIMLINTS GVAEYSTNKK
DLYLDFSKWG PFFQTITDMR MNDTFRLDRA VRGFDSDNPW RIFGYQPTPD HQYLIQTTYR
IYDDYTKERS ELSLHALVTQ VLNQHPWVLA LDLIGSTGMI TSQLDENPVQ ADPHDAEIAQ
DVYTTHETRD FPDERNQTLT RFFFIESGDN VSPASAYIDH VAKIVYSTQH YEQEKGSLLT
LAISLILIAI ILAFALAYLL SRYIFSPVDT LLADLDEISR GNLNHQIRPS RHLEINRIND
AVSRMVESIR GSIRSLEISE KRYSTLFSNA SDAIILWNGE RVIHANPAAF TLFGWDENIR
ERAGSTPNEI IRCILQRKNP EEDEWNMNTD ISGKGACTLN IRLVRLVLED LPMDLIQIRD
ITRETRMHEE IHRLADIVKN TQAGIMAGPV HAPDIVNKAY ARIHGCTPEE AIEGGFFGFI
HPDYKEDIPV WIRIATERGH MTGEAIRVRK DGSEFPALHD LTIVTDAHHE PYLILNVQDI
SDQIKVWNLT LEKEALSDSL NLLSGILDSL PDPTFVIDIS GHVLAWNKAM TVISGRSEEE
IRAGKMSHAQ AVYGEDRPML IDKIIRPDLD ISRYYTNVNE ENGIYSAEVI NHDREGKIRY
KWAIAGPLYD SKGSMIGAIE TIRDITELKE AMKKESELAN KLMLLSSLTR HDIRNKVTVI
DGFRFFAESE TDNPKIKEIL AHQKNAIQDI GKLIDFSKAY QEIGIHEPVW HNVRELFERA
VRQVSIDLKV VCDIPSLEVY ADALIYQVFY NLAENSLRHG DHVTTIRLYV DLSGESPLLI
YEDDGQGIVD TQKEQIFLRG YGKNTGLGLF LIREILAITG ITIVEHGIYG QGVRFEMKIP
PDHFRFTDQM EQNL
//
