ID B8GGK7_METPE Unreviewed; 1267 AA.
AC B8GGK7;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Mpal_0908 {ECO:0000313|EMBL:ACL16262.1};
OS Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanosphaerula.
OX NCBI_TaxID=521011 {ECO:0000313|EMBL:ACL16262.1, ECO:0000313|Proteomes:UP000002457};
RN [1] {ECO:0000313|EMBL:ACL16262.1, ECO:0000313|Proteomes:UP000002457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1556 / DSM 19958 / E1-9c
RC {ECO:0000313|Proteomes:UP000002457};
RX PubMed=26543115; DOI=10.1128/genomea.01280-15;
RA Cadillo-Quiroz H., Browne P., Kyrpides N., Woyke T., Goodwin L., Detter C.,
RA Yavitt J.B., Zinder S.H.;
RT "Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a
RT Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.";
RL Genome Announc. 3:e01280-15(2015).
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; CP001338; ACL16262.1; -; Genomic_DNA.
DR RefSeq; WP_012617581.1; NC_011832.1.
DR AlphaFoldDB; B8GGK7; -.
DR STRING; 521011.Mpal_0908; -.
DR GeneID; 25394113; -.
DR KEGG; mpl:Mpal_0908; -.
DR eggNOG; arCOG02358; Archaea.
DR eggNOG; arCOG06712; Archaea.
DR HOGENOM; CLU_264256_0_0_2; -.
DR OrthoDB; 106882at2157; -.
DR Proteomes; UP000002457; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 4.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 6.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR036097; HisK_dim/P_sf.
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; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 6.
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; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 3.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 6.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 6.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 5.
DR PROSITE; PS50112; PAS; 4.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ACL16262.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002457};
KW Transferase {ECO:0000313|EMBL:ACL16262.1}.
FT DOMAIN 25..96
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 99..151
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 403..454
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 490..543
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 563..616
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 617..689
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 693..745
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 781..834
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 854..907
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1052..1266
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 445..490
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 736..781
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1267 AA; 144652 MW; 82006C2EFA91FCE4 CRC64;
MSEELQANND QLLANERALL ESLERNTFLS DILDRSSQPF GVGYLDGRLG IVNHAFEELT
GYTADELQKM DWTATLTPPE WLDVERKNLE ELHRTGKPVR YEKEYIKKDG TRVAIELLVH
LVTDKEGNPQ YYYSFITDIT EQKRNREILS LSNRVLHSAE EHHTLQPLLE EYIRTLQEYT
GCDSIGVRIL DEQGNIPYLA YAGFSRDFYE QENPLSVRTD HCICINVIEG TTDPSLPFYT
AGGSFMINAT TKFRATESDE EKEKTRNTCT MVGYESVALI PIRKGDQIMG LLHLADHQEG
MISAEKVRVL EQVAYALGAS IVRVQTEEAL RKQEKTAQAI LAAAKESIWL FGTDDTILMA
NPTALVRLGG KDTGEVIGHQ YSEFMTSELA QARRARIEEV ISSRRSVQFE DIRAGTIFIH
TFCPVFDEAG AVSSIAAFSR DITGIRQADE ELLKKNEGLH ILNEELTATQ EELRQSIDEL
TTMEHELRET GQYLENLIQY ANAPIIVWDP AFRITRFNHA FELLIGRKAA DVIGQPLELL
FPKKFAEPVL EIIRKTTRGE RMEVVEIPIL HQNGEIRTVL WNSAAIFGSD GETVLSTIAQ
GQDITERKRT EEALHEAHLR LTHHIENSPL AVVEFDAQFR VTRWSDEAEK VFGWTMAEVM
GRTIDEIPWV YEEDVDRVAS ISADMMNGKA PRNKHTNRNY RKDGAVITCE WYNSALRDET
GELVSILSQV LDVTERDRAE ADLLEKNQEL SELNEELTAT QEELRQSIDE LTTMEHELRE
TGQYLENLIQ YANAPIIVWD PAFRITRFNH AFELLIGRKA ADVIGQPLEL LFPKKFAEPV
LEIIRKTNDG ERMEVVEIPI LHQNGEVRTV LWNSAAIFGA DGETVQSTIA QGQDITKRKW
AEEALRQSEE QYRMLFNTLT EGFCIIEMLF DADERPIDYR FLEINPAFER QTGLHEAQGR
LMRDLAPNHE EHWFEIYGTI ALTGEPVRFE NEAKALNRWY EVSAYRVGGP ESRRVAILFN
DITERKQAEE VLKTIADNLK ASNQELEQFA YIASHDLKEP LRMVTCFSQI LERQYKGQLD
ADADEFIGYI VDGALRMEAL INDLLLYSRI NQGMRPVERV DMKHAIEEAI SNLIIPIRER
NARITRGAMP SIQGDLSQMV QLFQNLIGNA MKYCPEEREP EIWINAERTG KGWTFSVKDN
GLGIDPAYHE QIFMIFRRLH TKAEYPGTGI GLAVVKRIVE RHGGRIWVES EEGSGSTFLF
TIPEKPL
//
