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Database: UniProt
Entry: A0A196R018_9RHOB
LinkDB: A0A196R018_9RHOB
Original site: A0A196R018_9RHOB 
ID   A0A196R018_9RHOB        Unreviewed;       740 AA.
AC   A0A196R018;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=A8B74_00315 {ECO:0000313|EMBL:OAN98132.1};
OS   Sulfitobacter geojensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Sulfitobacter.
OX   NCBI_TaxID=1342299 {ECO:0000313|EMBL:OAN98132.1, ECO:0000313|Proteomes:UP000078317};
RN   [1] {ECO:0000313|Proteomes:UP000078317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EhN01 {ECO:0000313|Proteomes:UP000078317};
RA   Rosana A., Orata F., Boucher Y., Case R.;
RL   Submitted (MAY-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAN98132.1}.
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DR   EMBL; LXYM01000001; OAN98132.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A196R018; -.
DR   STRING; 1342299.Z947_2588; -.
DR   eggNOG; COG5000; Bacteria.
DR   Proteomes; UP000078317; 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   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   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, ECO:0000313|EMBL:OAN98132.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078317};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        56..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        87..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        290..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          312..365
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          377..418
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          502..727
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   740 AA;  81358 MW;  8D86F104F951E3CE CRC64;
     MERLGRLRRL KRVRNLSTLG LVVLGPVLAM ATYLALGPLG QGANTLSLRL VLLTDLVYVL
     LVAALVLSQV ARLIAARRAK SAGSRLHLRL TGVFALMALI PTVTVAVFAG LTVNVGLEGW
     FSDRVRGVVG SSLAAAQAYE AEQRQDLIED ARALARNIDN ARNQGINLSD SQLLGEGQRQ
     IQRGLREAYL IDSTAEIRAR GDRSYLFDYE KPTGAQLTAA ADQGLLVIED WPNNEFRALV
     PMQSFLDRYL YVSRDVDGKI LSLLDETTET VRLYQQLESD RGRLLFEFGL LYLGFAVILI
     LAAVWLGLWF AERLSGPVGR LTGAAQQVGA GNLNVQVREE DGDDEIAMLG RYFNQMTKQL
     QGQRETLLDN TRQIERRRRL FDSVLSSVTS GVVGLDPEGR VTFVNRSAMR LLDWSEEQQS
     VSLSVAVPEF GPLFETISAK QGDTAQEEIK VSRQGAMENL LVRMATRRTG DGRLEGYVVA
     FDDVTDLVSA QRMAAWGDVA QRIAHEIKNP LTPIQLSAER IRRKFAPKLG DDSDSLEQMT
     GVIIRQTGDL RRIVDEFSKF ARMPEPETSE HNLTQLVKDA VFLQQSGQPE VKILSDLGEG
     VVMADIDATM ISQALNNLIK NAGEAIESLQ KSDAPENLKP QIRVTLQHSD ASATLTIADN
     GIGLPEDRAR LFEPYVTTRS EGTGLGLPIV KKIIEEHGGT LTLDNAPVFE GQDHFGAMAV
     ISLPLVPSPQ PAKRVETADE
//
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