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Database: UniProt
Entry: A0A0A1MRV7_9BACI
LinkDB: A0A0A1MRV7_9BACI
Original site: A0A0A1MRV7_9BACI 
ID   A0A0A1MRV7_9BACI        Unreviewed;       538 AA.
AC   A0A0A1MRV7;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=citS_1 {ECO:0000313|EMBL:CEI82429.1};
GN   ORFNames=BN997_02295 {ECO:0000313|EMBL:CEI82429.1};
OS   Oceanobacillus oncorhynchi.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=545501 {ECO:0000313|EMBL:CEI82429.1, ECO:0000313|Proteomes:UP000040453};
RN   [1] {ECO:0000313|EMBL:CEI82429.1, ECO:0000313|Proteomes:UP000040453}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Oc5 {ECO:0000313|EMBL:CEI82429.1,
RC   ECO:0000313|Proteomes:UP000040453};
RA   Urmite Genomes Urmite Genomes;
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CDGG01000001; CEI82429.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A1MRV7; -.
DR   STRING; 545501.BN997_02295; -.
DR   Proteomes; UP000040453; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR033463; sCache_3.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR016120; Sig_transdc_His_kin_SpoOB.
DR   InterPro; IPR039506; SPOB_a.
DR   PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF17203; sCache_3_2; 1.
DR   Pfam; PF14689; SPOB_a; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   SUPFAM; SSF103190; Sensory domain-like; 1.
DR   SUPFAM; SSF55890; Sporulation response regulatory protein Spo0B; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000040453};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        17..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          340..533
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   538 AA;  60018 MW;  33AC18C9628BFAB5 CRC64;
     MIIIINRLNQ VNLLTKILVL IIGLILFVTI LLTAFYSYME VEMTEEEIGE QALQTAQMVA
     NIPSIREGFS QASPEETIQP IAEEMRKLTG AEFIVIGNTE GIRYSHPDQD KLGKNMVGGD
     NDAALIDGES YVSRAEGSLG PSLRGKTPVW NYEGDIVGVV SVGYMIKDIN ATILSNIKKL
     ILPSVIVLFV GTIGGLLLTR NIRGQLMGFE PHKITSLYRE RNAILSAIHE GMIAVNEDGV
     IQLMNQSAEK LLSGKQKAFF NQPISKVLPE LPLSSLIKNG QVCRNKQVEV NDRHIIFNMV
     PIYNQNQVRG AVLSFRDKTE LKEIIDTLGE VRSYSEELRA QTHEYTNRLY VLSGMLQLGN
     FEEAIELIQK ETQTVETQNK IVYDQISDKT IQAILLGKIG KASELKINFL IDDYSSLSEM
     ADYIEPTNLI TILGNVIDNA LDAVRETENG TVQFFSTDIG HDYIFEVADN GVGIGKKDIH
     RIFHRRFSTK DKTTRGYGLA MVKETIENLN GRIEVKSNLA EGTIFTIFIP KQQAKKTG
//
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