ID F0T8Z0_METLA Unreviewed; 1257 AA.
AC F0T8Z0;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Signal transduction histidine kinase {ECO:0000313|EMBL:ADZ09818.1};
GN OrderedLocusNames=Metbo_1591 {ECO:0000313|EMBL:ADZ09818.1};
OS Methanobacterium lacus (strain AL-21).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX NCBI_TaxID=877455 {ECO:0000313|EMBL:ADZ09818.1, ECO:0000313|Proteomes:UP000007490};
RN [1] {ECO:0000313|Proteomes:UP000007490}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AL-21 {ECO:0000313|Proteomes:UP000007490};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Cadillo-Quiroz H.,
RA Imachi H., Zinder S., Liu W., Woyke T.;
RT "Complete sequence of Methanobacterium sp. AL-21.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADZ09818.1, ECO:0000313|Proteomes:UP000007490}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AL-21 {ECO:0000313|EMBL:ADZ09818.1,
RC ECO:0000313|Proteomes:UP000007490};
RX PubMed=24449792; DOI=10.1099/ijs.0.059964-0;
RA Cadillo-Quiroz H., Brauer S.L., Goodson N., Yavitt J.B., Zinder S.H.;
RT "Methanobacterium paludis sp. nov. and a novel strain of Methanobacterium
RT lacus isolated from northern peatlands.";
RL Int. J. Syst. Evol. Microbiol. 64:1473-1480(2014).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002551; ADZ09818.1; -; Genomic_DNA.
DR RefSeq; WP_013645169.1; NC_015216.1.
DR AlphaFoldDB; F0T8Z0; -.
DR STRING; 877455.Metbo_1591; -.
DR GeneID; 10278048; -.
DR KEGG; mel:Metbo_1591; -.
DR eggNOG; arCOG02276; Archaea.
DR eggNOG; arCOG02348; Archaea.
DR eggNOG; arCOG06537; Archaea.
DR eggNOG; arCOG06712; Archaea.
DR HOGENOM; CLU_265168_0_0_2; -.
DR OrthoDB; 8127at2157; -.
DR Proteomes; UP000007490; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00130; PAS; 5.
DR CDD; cd17534; REC_DC-like; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; IPR011006; CheY-like_superfamily.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR011495; Sig_transdc_His_kin_sub2_dim/P.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 6.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065:SF23; SENSOR HISTIDINE KINASE PDTAS-RELATED; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07568; HisKA_2; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 3.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 6.
DR SMART; SM00091; PAS; 6.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 6.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 5.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ADZ09818.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000007490};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..119
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 131..203
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 203..254
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 432..469
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 551..621
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 674..727
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 745..796
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 874..924
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 925..995
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1163..1252
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 534..561
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 55
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1257 AA; 143761 MW; 98F8FB1F244677B2 CRC64;
MAGKKILIVE DETVEALDIK KMLESFGYDV PSVVLNGAIA VETAKKIRPD LILMDIVLKG
ELDGINAAKK IKELNIPVIF LTAHSDNEAV ERAKKTEPYG YIVKPYDPID LKNTVEFALY
RHSMDEKLKK SEKKYRNIIE NLQDAYLRAD NKGTIIMASP SAARMFNYSS SKEMIGQSVL
TIYSDPDTRN LMLEQLEKHS KLEGYEFEGL RKDGTTFWLS MNSQPYHETN KVMGVESFLR
DITEPKESEK KIEKLYRLYA TLSQINQAVV RINDQESFFK IICNVCIEFG KFKMAWIGSV
DEATGKVTPL VHTGSESGYL DTVDVNVKKL NSPSNRAMKT KKFILIKDVR EELNRPWVKE
AIKRDFNSMV VIPIKLKARV IAMLYIYSSE VNFFTHEELD LIREMAMDIS FAITTLNSEK
ERKLLSRALI ESEESYRELV DNSIVAIYKT NLEGNILFAN NAMAEFFGFK SIKELFKTNV
KDLYMDINDR KVLMDRLLFE GSIKQCEVEM ATQTGTPVSI LLSAKLNDDE ISGMMMDISQ
LKEVEAELKN SENKFRALVE NASDALLVHD YDGNFVDINK KASESLGYTR EEFLHMNVAD
IDPDFDLETA RKTWKSIIPG SSNTIYRNQI RKDGTQFPVE ISFATVDIEG KKLYMGLCRD
MTDRINSEKE LKASEEKYHS IFDYSMDAII LSVVNEKITD ANHAAVELFG YSKEEFLQLS
RNDLIDPGEE TNHIFHTNTN LNSYYQVELN LRKKDGTKFT AELLSSNYYD RAGNEKSVTQ
IRDISPRKIA EKRIKESENR YRKVGQLISD FAYSCKQDSD GIYKNEWITD SFFNITGFNK
QKLLKHGNWL FTVHPNDEEI AVNQLNKLKP GETSVENFRI ITNHGKIIWL ENHLECVEDN
GNLRLYGAAK DITEIERTAS ELKLNEEKFK AIINNSSDLI RILDKNCKIV FDSPSSTRIL
GYPEGSLVGT SPLELIHPDD RDQVESDLEE VYKNKNPGTP SEFRILKSDG TYLPVESVAQ
NMFNVPSVKG IVVTTHPIKQ RKEMENAIKS SLNEKEILLK EIHHRVKNNM QIISSLLNLQ
KEYVDDLEAI NVLQESQNRV KTMSIIHEKL YQSDDLTHIN IQEYVEKLTN DLMYSYAATN
VNPFIDINNI KMNIETALPC GLIISELVSN SLKYAYSKDK NNELKISLKK YGDLFELVIS
DNGIGLPENL DFKNTESLGL QLVNNLVGQL DGEIKLNQDH GAEFKIVFKE LQYKPRI
//