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Database: UniProt
Entry: I0HRI0_RUBGI
LinkDB: I0HRI0_RUBGI
Original site: I0HRI0_RUBGI 
ID   I0HRI0_RUBGI            Unreviewed;       754 AA.
AC   I0HRI0;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=RGE_22760 {ECO:0000313|EMBL:BAL95617.1};
OS   Rubrivivax gelatinosus (strain NBRC 100245 / IL144).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Rubrivivax.
OX   NCBI_TaxID=983917 {ECO:0000313|EMBL:BAL95617.1, ECO:0000313|Proteomes:UP000007883};
RN   [1] {ECO:0000313|EMBL:BAL95617.1, ECO:0000313|Proteomes:UP000007883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100245 / IL144 {ECO:0000313|Proteomes:UP000007883};
RX   PubMed=22689232; DOI=10.1128/JB.00511-12;
RA   Nagashima S., Kamimura A., Shimizu T., Nakamura-isaki S., Aono E.,
RA   Sakamoto K., Ichikawa N., Nakazawa H., Sekine M., Yamazaki S., Fujita N.,
RA   Shimada K., Hanada S., Nagashima K.V.P.;
RT   "Complete genome sequence of phototrophic betaproteobacterium Rubrivivax
RT   gelatinosus IL144.";
RL   J. Bacteriol. 194:3541-3542(2012).
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; AP012320; BAL95617.1; -; Genomic_DNA.
DR   RefSeq; WP_014428479.1; NC_017075.1.
DR   AlphaFoldDB; I0HRI0; -.
DR   STRING; 983917.RGE_22760; -.
DR   KEGG; rge:RGE_22760; -.
DR   PATRIC; fig|983917.3.peg.2206; -.
DR   eggNOG; COG4251; Bacteria.
DR   HOGENOM; CLU_000445_114_71_4; -.
DR   Proteomes; UP000007883; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 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; IPR033479; dCache_1.
DR   InterPro; IPR003660; HAMP_dom.
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; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR42878:SF7; BACTERIOPHYTOCHROME; 1.
DR   PANTHER; PTHR42878; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02743; dCache_1; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAL95617.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007883};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAL95617.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        295..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          315..369
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          451..501
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          530..744
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          489..523
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   754 AA;  80856 MW;  FA3CF16D2F45A6CC CRC64;
     MLPRWTDPRR SLRARFALLL GGSGLALALV TAAVVGIVQR GQLVEQQGYS MRREALLLAR
     VLDGALRQRL EQLQATADQP LLASGLFDPG DARLLLEGLR AQQPAFAWIA IVAPDGQVRV
     ATNALLEGAD LQAEPWFAPA AHAPWIGSRR PAGALTASLG LVDGQPPQLI DMGLPMTDTA
     GRTTGVLVAR LRWDWLRELH RSLKNDLNVD NGIESAVLDR DGRVLLGPPA WLDRPPAVPP
     DPEADPGLVT WPGEGEFLSD WERSPGGEGA SGLVVLLRQP AALAFQPAIE MSRRLLLLGA
     LGTAAFMLLS LWLAARVARP IGELSAAALR VVHDQPPQFA AIPPEREDEV AEVAHALRRL
     HDTLARRLAE QQLATARYET LFRDAPVAIY LAIEDHLLIA NQACVRLFGA PGADALVGLD
     TAGLFHTDDA GLAELRLRQQ AALEPGGAPT PTLEHRIRRL DGGIAEVEST AIGLALAEGR
     GVQVVLHDIT EQRQAQAALR ELNAQLEARV AARTAELQGA NAELDAFAYA VSHDLRAPLR
     AMTGFSQALI EDHGAELPPP ARGYLDQIVL AGQRMGDLVE GLLTLSRTLR GALSVAPVDL
     SALAEQTLAD LRRAEPGREV AVEIEPGLVA TGDRRMLAAL VNNLVGNAWK YTAGCAGARI
     RVFSIIDDGS RWICVEDNGA GFDMAHAGRL FKAFARLHRQ DEFPGLGIGL ATVQRIVHRH
     GGRIEAEGSP GRGARFRFTL PERPRAGVNE GATA
//
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