ID   A7I5B1_METB6            Unreviewed;       766 AA.
AC   A7I5B1;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Mboo_0402 {ECO:0000313|EMBL:ABS54922.1};
OS   Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX   NCBI_TaxID=456442 {ECO:0000313|EMBL:ABS54922.1, ECO:0000313|Proteomes:UP000002408};
RN   [1] {ECO:0000313|Proteomes:UP000002408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21154 / JCM 14090 / 6A8
RC   {ECO:0000313|Proteomes:UP000002408};
RX   PubMed=25998264; DOI=10.1099/mic.0.000117;
RA   Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L.,
RA   Detter C., Podell S., Yavitt J.B., Zinder S.H.;
RT   "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic
RT   peatland environments.";
RL   Microbiology 161:1572-1581(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; CP000780; ABS54922.1; -; Genomic_DNA.
DR   RefSeq; WP_011991410.1; NC_009712.1.
DR   AlphaFoldDB; A7I5B1; -.
DR   STRING; 456442.Mboo_0402; -.
DR   GeneID; 25393895; -.
DR   KEGG; mbn:Mboo_0402; -.
DR   eggNOG; arCOG02385; Archaea.
DR   eggNOG; arCOG06192; Archaea.
DR   eggNOG; arCOG06193; Archaea.
DR   HOGENOM; CLU_000445_114_58_2; -.
DR   OrthoDB; 116661at2157; -.
DR   Proteomes; UP000002408; Chromosome.
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   CDD; cd00130; PAS; 1.
DR   CDD; cd00156; REC; 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; 3.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF13426; PAS_9; 2.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00091; PAS; 3.
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; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ABS54922.1};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002408};
KW   Transferase {ECO:0000313|EMBL:ABS54922.1}.
FT   DOMAIN          3..118
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          134..179
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          222..274
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          661..760
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          265..292
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         53
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   766 AA;  85080 MW;  2DD427727933CD58 CRC64;
     MYRILYVDDE PGLLEIGKLF LDSTGEFDVS TLTSAEKALE SPEILLFDAI ISDYQMPGMD
     GISFLKNIRK RTKDVPFVLF TGRGREEVVI EAINSGADFY LQKGGQPTAQ FAELAHKIRI
     AIERRRAIDS VKDSEQRLTD IIDFLPDATF AIDTTGRVIA WNRAMEQMTG TPAEDIRGKG
     NYEDGMAFYG ERRPMLADLL LNPDFSFEEK TYTNVRRAGT GITAEGPVQI RGNSLRYLWG
     IAGRLFDKEG KCTGSIESIR DITERKEAEK ELQAAYEQIA AAEEELRGQY EELAAGDLKL
     KEREAQLWAI FKEAPHAIAI SDSATGKYLS VNTLFEQGSG LAASEILGKT SAEIGFVPPE
     EHELLLKEFI REGGIRQKPL TAKMWDGRKA DILFTAVPIV LSTRTIVLTM VVDITDMKRI
     EDALRKQEQI LNDAFASIKD GISLLDKTMT VIRVNKTMEE WYSHEMPLIG RKCWEVYHGR
     AGPCDICPTL HTLKEGKPAK ERVPLVDAGE VTGWLDLYSY PVIDSATGEM TGVIEYVRNV
     TEETKAQRDL ELANKKLNLL SSTTRHDILN TLTGLQGLVD KAASLSTSGE CTHLLSQIRD
     RAGIIRQQID FTGRYQEVGV HAPLWQDVNV LLSRILPATP RTKAGIVNDC DNVEIFSDPL
     LEKVLYNLVN NALKYGGPDL TTVHITSDLS APELIIAVAD DGVGIAAGDK DHLFQREVGQ
     KTGSGLFLAR EILSITGITI RETGTPGKGA RFEILVPPEA WRKKRQ
//