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Database: UniProt
Entry: A0A1Y5TFH8_9RHOB
LinkDB: A0A1Y5TFH8_9RHOB
Original site: A0A1Y5TFH8_9RHOB 
ID   A0A1Y5TFH8_9RHOB        Unreviewed;       586 AA.
AC   A0A1Y5TFH8;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=dctB_2 {ECO:0000313|EMBL:SLN62611.1};
GN   ORFNames=PEL8287_03420 {ECO:0000313|EMBL:SLN62611.1};
OS   Roseovarius litorisediminis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=1312363 {ECO:0000313|EMBL:SLN62611.1, ECO:0000313|Proteomes:UP000193827};
RN   [1] {ECO:0000313|EMBL:SLN62611.1, ECO:0000313|Proteomes:UP000193827}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8287 {ECO:0000313|EMBL:SLN62611.1,
RC   ECO:0000313|Proteomes:UP000193827};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-2017) 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};
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DR   EMBL; FWFL01000010; SLN62611.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y5TFH8; -.
DR   OrthoDB; 7568856at2; -.
DR   Proteomes; UP000193827; Unassembled WGS sequence.
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; cd18773; PDC1_HK_sensor; 1.
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; 1.
DR   InterPro; IPR029150; dCache_3.
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; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR017055; Sig_transdc_His_kinase_DctB.
DR   PANTHER; PTHR43065:SF58; C4-DICARBOXYLATE TRANSPORT SENSOR PROTEIN DCTB; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF14827; dCache_3; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PIRSF; PIRSF036431; STHK_DctB; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
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; SSF103190; Sensory domain-like; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193827};
KW   Transferase {ECO:0000313|EMBL:SLN62611.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        288..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          369..579
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          316..360
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   586 AA;  64845 MW;  A2E8BAB1557E000E CRC64;
     MANTPATISL NRMRPRRWRV RIVLILLIAL AVSIVLFTNK LLTDRFTENT RNRAELRLVL
     YSGNLLSELR QNAIVPQLLA RDPTLISALN TGDYAQSTQR LISFLDEIGA ASLTLLDNEG
     RTVASTVRNS LGQSLKQAPY YVDALRSSDT VFKVLKQETG QYNFYYSRRI ESQNELVGVI
     VVEVDLRKYE RAWAGISDAV LVTDTEGRII LATEPRWRGL SEADALAREP VNSAIQRAIQ
     ATADWTTLPA DAYLQGEAVM RVEGRVAFRG WRIASFTTYA SVREKVNGVL ALEIMAFAIL
     LALAFYFLNR KTAVRMALFQ RESAELRALN ARLQREIAER ERVQENLAVA EQTLAQSSKL
     AALGEMSAAV SHELNQPLAA MKTYLAGARL LLNRHRPDEA LSSFQRIDDL IERMGAITKQ
     LKSYARHSGD TFEPVNMGDA LASALSMMEP QLRQGRVKIT RALPSEPVMV MADRVRVEQV
     MINLLRNAMD ATENVEDATV DILLAAGETA MLTVRDNGYG INDFDKLFEP FYTTKQPGDG
     VGLGLAISSG IVNDLGGRLT ARNAAGGGAV FEVQLPILPE ETRAAE
//
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