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Database: UniProt
Entry: A7I735_METB6
LinkDB: A7I735_METB6
Original site: A7I735_METB6 
ID   A7I735_METB6            Unreviewed;       335 AA.
AC   A7I735;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Mboo_1028 {ECO:0000313|EMBL:ABS55546.1};
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:ABS55546.1, 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; ABS55546.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7I735; -.
DR   STRING; 456442.Mboo_1028; -.
DR   KEGG; mbn:Mboo_1028; -.
DR   eggNOG; arCOG06193; Archaea.
DR   HOGENOM; CLU_827967_0_0_2; -.
DR   Proteomes; UP000002408; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00075; HATPase; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ABS55546.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002408};
KW   Transferase {ECO:0000313|EMBL:ABS55546.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        37..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        74..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          233..331
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   335 AA;  38202 MW;  8A013527C8A9764A CRC64;
     MGRCGQSCPS EQLSLLPRSF KMYGNMAKPF RQHYESFLRY APLSIVGVCL LASVGWIAAS
     DYLTYYFVRG NQNFFMISIA ADLAYICFIT VFLYVAIRYY LNEIQTVNRR AYETLKQSEQ
     DCRITNHKLH LMTDIAYQDI QNKINSVIAF SDMSRSKTPE QREAFRQKGV QQLKQVLDLI
     AKTKDYQQMG VERETWVDVQ ETVKTQWAHV DSPPGVTMSA DVHGLRIYTD PVIERVFFNL
     MSNAIKHGKT TKHISVSVEE TDGGAVLRFE DNGIGIAAAH KPQIFERIVG GPGKFHLFFV
     RECLTLYGMS IAETGEEGKG ARFEIRIPWK MCQVA
//
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