ID   DCTB_RHILE              Reviewed;         622 AA.
AC   P10047;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   25-MAY-2022, entry version 130.
DE   RecName: Full=C4-dicarboxylate transport sensor protein DctB;
DE            EC=2.7.13.3;
GN   Name=dctB;
OS   Rhizobium leguminosarum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3671068; DOI=10.1093/nar/15.19.7921;
RA   Ronson C.W., Astwood P.M., Nixon B.T., Ausubel F.M.;
RT   "Deduced products of C4-dicarboxylate transport regulatory genes of
RT   Rhizobium leguminosarum are homologous to nitrogen regulatory gene
RT   products.";
RL   Nucleic Acids Res. 15:7921-7934(1987).
CC   -!- FUNCTION: Member of the two-component regulatory system DctB/DctD
CC       involved in the transport of C4-dicarboxylates. DctB functions as a
CC       membrane-associated protein kinase that phosphorylates DctD in response
CC       to environmental signals.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
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DR   EMBL; X06253; CAA29595.1; -; Genomic_DNA.
DR   EMBL; Z11529; CAA77619.1; -; Genomic_DNA.
DR   PIR; A26981; A26981.
DR   RefSeq; WP_018242999.1; NZ_WXXP01000006.1.
DR   AlphaFoldDB; P10047; -.
DR   SMR; P10047; -.
DR   STRING; 936136.ARRT01000006_gene4359; -.
DR   eggNOG; COG4191; Bacteria.
DR   BRENDA; 2.7.13.3; 5343.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma 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   CDD; cd00082; HisKA; 1.
DR   Gene3D; 3.30.565.10; -; 1.
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   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; SSF103190; SSF103190; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..622
FT                   /note="C4-dicarboxylate transport sensor protein DctB"
FT                   /id="PRO_0000074747"
FT   TOPO_DOM        1..24
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        25..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        43..320
FT                   /note="Periplasmic"
FT   TRANSMEM        321..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        339..622
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          412..622
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         415
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   622 AA;  67682 MW;  8FF3B97C2235058F CRC64;
     MHKSAMSVSQ KLWPSLPLQH RIRRMWWTYA ALAFLAVVAS LWTSGEIGQH RAEAALEEQA
     RMDVTLNAAL LRTVLEKYRA LPFVLSQDTA LAAALVGNDA GTFERLSQKL EILAAGTKAA
     VIYVIDKDGI AVSASNWREP TSFVGNDYRF REYFQGAVER GQAEHFALGT VSKKPGLYIS
     QRISGSNGLL GVVVVKVEFD DVEADWNASG TPSYVVDERG IVLITSLPSW RFMTIGRIAE
     DRLTAIRESL QFGAAPLQPL PLDMVRNLGE GLDVVEIVMP GDAGKTRFLD VATSVPATGW
     HLQHLVALGP SVDAGIREAR MLALLILLPL LAGAAFLLRR RHTIALRISS EQQAREELER
     RVVERTLDLS QARDRLQAEI IGHKSTEQKL QAVQQDLVQA NRLAILGQVA AGVAHEINQP
     VATIRAYADN ARTFLDRGQT APAGENLESI AALTERIGSI TEELKTFARK GRGSAEPTGL
     KDVIEGAVML LRSRFAGRMD TLDIDLPPDE LQVMGNRIRL EQVLINLLQN ALEAVAPKAG
     EGRVEIRTST DAGMVTVTVA DNGPGIPTEI RKGLFTPFNT SKESGLGLGL VISKDIVGDY
     GGRMDVASDS GGTRFIVQLR KA