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Database: UniProt
Entry: B6AX27_9RHOB
LinkDB: B6AX27_9RHOB
Original site: B6AX27_9RHOB 
ID   B6AX27_9RHOB            Unreviewed;       752 AA.
AC   B6AX27;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=ntrY {ECO:0000313|EMBL:EDZ42071.1};
GN   ORFNames=RB2083_1586 {ECO:0000313|EMBL:EDZ42071.1};
OS   Rhodobacteraceae bacterium HTCC2083.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=314270 {ECO:0000313|EMBL:EDZ42071.1, ECO:0000313|Proteomes:UP000005746};
RN   [1] {ECO:0000313|Proteomes:UP000005746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2083 {ECO:0000313|Proteomes:UP000005746};
RX   PubMed=21036993; DOI=10.1128/JB.01268-10;
RA   Kang I., Vergin K.L., Oh H.M., Choi A., Giovannoni S.J., Cho J.C.;
RT   "Genome sequence of strain HTCC2083, a novel member of the marine clade
RT   Roseobacter.";
RL   J. Bacteriol. 193:319-320(2011).
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; DS995276; EDZ42071.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6AX27; -.
DR   STRING; 314270.RB2083_1586; -.
DR   eggNOG; COG5000; Bacteria.
DR   HOGENOM; CLU_019564_1_0_5; -.
DR   Proteomes; UP000005746; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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   CDD; cd06225; HAMP; 1.
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; 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; IPR017232; NtrY.
DR   InterPro; IPR045671; NtrY-like_N.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF19312; NtrY_N; 1.
DR   Pfam; PF00989; PAS; 1.
DR   PIRSF; PIRSF037532; STHK_NtrY; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 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; PS50112; PAS; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005746};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        69..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        109..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        314..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          336..389
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          401..442
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          526..751
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   752 AA;  83745 MW;  DBADB94F71991F39 CRC64;
     MSQPVTPPAP AKLARRKKLS LWMRLSHLRR QRRVQNAITL GVVLLGPMLA FATFLVLGPL
     DQDVGGPGLR FVLLLDLVYV LVVAALVLQR VAQMIAARRA HSAGSRLHLR LTGVFALMAL
     IPTVTVAIFA GITINMGLEA WFSQRVQRVV GNSLAAAQAY ENEQRRDLQE DAQALANYLN
     ARRGEVRFMR TASLGEVLRD GQLQIQRGLR EAFVVDGTGE IKARGDRSYM FDFDPLAPIE
     IETARTDGIL ILKDWENNEF RAVVNLVGYL NEYLYVSREV DGSILKLLDE TQETALFYQQ
     QESERGRRLF EFGLVYIGFA VILILAAVWL GLWFAERLSR PVGRLAGAAQ RVGAGNLDVQ
     VLEEEGDDEI AMLGRYFNQM TRQLKGQRNT LVENNRQIER RRRMFDSVLS SVSSGVVGLD
     ESGRISFVNR SAERLLGWHQ DKQDVDLSVA VPEFGPLLDK LRNGQMGNTQ GEIKVSRDGQ
     LENLLVRMSR RLRDDGTLEG FVVAFDDVTD LVTAQRMAAW GDVARRIAHE IKNPLTPIQL
     SAERIQRKFM PQVGDDAERL EQMTGVIIRQ TGDLRRIVDE FSKFARMPEP DRRSGDLTQI
     VRDAVILQEA GQPDVIFDIN LPDTELLAEF DATMISQALT NLIKNAGEAI ASYIEKFEDA
     DVVCEVAISL TQDNNMALIQ IADSGIGLPE DRGRLFEPYV TTRDKGTGLG LPIVKKIIEE
     HGGSLILTDA PLMNGQGRPG AMAVVRLPLL DA
//
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