DCTB_RHIME
ID DCTB_RHIME Reviewed; 621 AA.
AC P13633;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 3.
DT 25-MAY-2022, entry version 169.
DE RecName: Full=C4-dicarboxylate transport sensor protein DctB;
DE EC=2.7.13.3;
GN Name=dctB; OrderedLocusNames=RB1524; ORFNames=SMb20612;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymB (megaplasmid 2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JJ1c10;
RX PubMed=2134335; DOI=10.1094/mpmi-3-174;
RA Watson R.J.;
RT "Analysis of the C4-dicarboxylate transport genes of Rhizobium meliloti:
RT nucleotide sequence and deduced products of dctA, dctB, and dctD.";
RL Mol. Plant Microbe Interact. 3:174-181(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=2793824; DOI=10.1128/jb.171.10.5244-5253.1989;
RA Jiang J., Gu B., Albright L.M., Nixon B.T.;
RT "Conservation between coding and regulatory elements of Rhizobium meliloti
RT and Rhizobium leguminosarum dct genes.";
RL J. Bacteriol. 171:5244-5253(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481431; DOI=10.1073/pnas.161294698;
RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT endosymbiont Sinorhizobium meliloti.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-185.
RC STRAIN=RCR2011 / SU47;
RX PubMed=2551890; DOI=10.1128/jb.171.10.5551-5560.1989;
RA Engelke T., Jording D., Kapp D., Puehler A.;
RT "Identification and sequence analysis of the Rhizobium meliloti dctA gene
RT encoding the C4-dicarboxylate carrier.";
RL J. Bacteriol. 171:5551-5560(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-177.
RX PubMed=2695394; DOI=10.1016/0378-1119(89)90473-3;
RA Wang Y.-P., Birkenhead K., Boesten B., Manian S., O'Gara F.;
RT "Genetic analysis and regulation of the Rhizobium meliloti genes
RT controlling C4-dicarboxylic acid transport.";
RL Gene 85:135-144(1989).
RN [7]
RP FUNCTION, AND AUTOPHOSPHORYLATION.
RX PubMed=7896073; DOI=10.1111/j.1574-6968.1995.tb07385.x;
RA Giblin L., Boesten B., Turk S., Hooykaas P., O'Gara F.;
RT "Signal transduction in the Rhizobium meliloti dicarboxylic acid transport
RT system.";
RL FEMS Microbiol. Lett. 126:25-30(1995).
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. {ECO:0000269|PubMed:7896073}.
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.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:7896073}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA26249.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAA63510.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAA63512.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=M33555; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; J03683; AAA63511.1; -; Genomic_DNA.
DR EMBL; J03683; AAA63510.1; ALT_INIT; Genomic_DNA.
DR EMBL; J03683; AAA63512.1; ALT_INIT; Genomic_DNA.
DR EMBL; M26531; AAA26249.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL591985; CAC49924.1; -; Genomic_DNA.
DR EMBL; M26399; AAA26251.2; -; Genomic_DNA.
DR EMBL; M33555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B33586; B33586.
DR PIR; D96032; D96032.
DR RefSeq; NP_438064.1; NC_003078.1.
DR RefSeq; WP_010976309.1; NC_003078.1.
DR PDB; 2ZBB; X-ray; 2.50 A; A/B/C/D=42-312.
DR PDB; 3E4O; X-ray; 2.30 A; A/B=42-312.
DR PDB; 3E4P; X-ray; 2.30 A; A/B=42-312.
DR PDB; 3E4Q; X-ray; 2.75 A; A/B=42-312.
DR PDB; 4GKG; X-ray; 1.70 A; A/F=350-395.
DR PDBsum; 2ZBB; -.
DR PDBsum; 3E4O; -.
DR PDBsum; 3E4P; -.
DR PDBsum; 3E4Q; -.
DR PDBsum; 4GKG; -.
DR AlphaFoldDB; P13633; -.
DR SMR; P13633; -.
DR STRING; 266834.SM_b20612; -.
DR EnsemblBacteria; CAC49924; CAC49924; SM_b20612.
DR GeneID; 61601427; -.
DR KEGG; sme:SM_b20612; -.
DR PATRIC; fig|266834.11.peg.6449; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_94_2_5; -.
DR OMA; SNWREPT; -.
DR BRENDA; 2.7.13.3; 5347.
DR EvolutionaryTrace; P13633; -.
DR Proteomes; UP000001976; Plasmid pSymB.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Plasmid; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..621
FT /note="C4-dicarboxylate transport sensor protein DctB"
FT /id="PRO_0000074748"
FT TOPO_DOM 1..26
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..320
FT /note="Periplasmic"
FT TRANSMEM 321..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..621
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 412..621
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"
FT CONFLICT 3
FT /note="H -> N (in Ref. 1 and 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="P -> Q (in Ref. 1; AAA63511/AAA63510)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="N -> K (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="L -> I (in Ref. 1; AAA63511/AAA63510)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="D -> N (in Ref. 1; AAA63511/AAA63510)"
FT /evidence="ECO:0000305"
FT CONFLICT 548..551
FT /note="EEAA -> KAAP (in Ref. 1; AAA63511/AAA63510)"
FT /evidence="ECO:0000305"
FT CONFLICT 615
FT /note="A -> T (in Ref. 1; AAA63511/AAA63510)"
FT /evidence="ECO:0000305"
FT HELIX 56..79
FT /evidence="ECO:0007829|PDB:3E4O"
FT HELIX 81..87
FT /evidence="ECO:0007829|PDB:3E4O"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:3E4O"
FT HELIX 101..117
FT /evidence="ECO:0007829|PDB:3E4O"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:3E4O"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:3E4O"
FT TURN 136..139
FT /evidence="ECO:0007829|PDB:3E4O"
FT HELIX 153..161
FT /evidence="ECO:0007829|PDB:3E4O"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:3E4O"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:3E4O"
FT STRAND 176..186
FT /evidence="ECO:0007829|PDB:3E4O"
FT STRAND 189..198
FT /evidence="ECO:0007829|PDB:3E4O"
FT HELIX 201..210
FT /evidence="ECO:0007829|PDB:3E4O"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:3E4O"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:3E4O"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:3E4O"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:3E4O"
FT HELIX 241..249
FT /evidence="ECO:0007829|PDB:3E4O"
FT TURN 250..255
FT /evidence="ECO:0007829|PDB:3E4O"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:3E4O"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:3E4O"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:3E4P"
FT STRAND 286..294
FT /evidence="ECO:0007829|PDB:3E4O"
FT TURN 296..299
FT /evidence="ECO:0007829|PDB:2ZBB"
FT STRAND 301..307
FT /evidence="ECO:0007829|PDB:3E4O"
FT HELIX 350..394
FT /evidence="ECO:0007829|PDB:4GKG"
SQ SEQUENCE 621 AA; 67133 MW; D60F724E2CA6BCC7 CRC64;
MHHVRMVKLP AEASDPHALR SRARRSWLVF AAVALVLLAA GLLLARDYGR SQALAGLAGQ
SRIDASLKAS LLRAVVERQR ALPLVLADDA AIRGALLSPD RPSLDRINRK LEALATSAEA
AVIYLIDRSG VAVAASNWQE PTSFVGNDYA FRDYFRLAVR DGMAEHFAMG TVSNRPGLYI
SRRVDGPGGP LGVIVAKLEF DGVEADWQAS GKPAYVTDRR GIVLITSLPS WRFMTTKPIA
EDRLAPIRES LQFGDAPLLP LPFRKIEARP DGSSTLDALL PGDSTAAFLR VETMVPSTNW
RLEQLSPLKA PLAAGAREAQ LLTLAALVPL LALAALLLRR RQVVAMRSAE ERLARNALEA
SVEERTRDLR MARDRLETEI ADHRQTTEKL QAVQQDLVQA NRLAILGQVA AGVAHEINQP
VATIRAYADN ARTFLHRGQT VTAAENMESI AELTERVGAI TDELRRFARK GHFAAGPTAM
KEVVEGALML LRSRFAGRMD AIRLDLPPDG LQALGNRIRL EQVLINLLQN ALEAIGDSED
GAIQVRCEEA AGGIALTVAD NGPGIAADVR EELFTPFNTS KEDGLGLGLA ISKEIVSDYG
GTIEVESGPS GTTFAVNLKK A
