[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=JJ1c10; PubMed=2134335 [NCBI, ExPASy, EBI, Israel, Japan] Watson R.J.; "Analysis of the C4-dicarboxylate transport genes of Rhizobium meliloti: nucleotide sequence and deduced products of dctA, dctB, and dctD."; Mol. Plant Microbe Interact. 3:174-181(1990).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=1021; PubMed=2793824 [NCBI, ExPASy, EBI, Israel, Japan] Jiang J., Gu B., Albright L.M., Nixon B.T.; "Conservation between coding and regulatory elements of Rhizobium meliloti and Rhizobium leguminosarum dct genes."; J. Bacteriol. 171:5244-5253(1989).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=1021; DOI=10.1073/pnas.161294698; PubMed=11481431 [NCBI, ExPASy, EBI, Israel, Japan] Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J., Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.; "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing endosymbiont Sinorhizobium meliloti."; Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-185. STRAIN=RCR2011 / SU47; PubMed=2551890 [NCBI, ExPASy, EBI, Israel, Japan] Engelke T., Jording D., Kapp D., Puehler A.; "Identification and sequence analysis of the Rhizobium meliloti dctA gene encoding the C4-dicarboxylate carrier."; J. Bacteriol. 171:5551-5560(1989).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-177. DOI=10.1016/0378-1119(89)90473-3; PubMed=2695394 [NCBI, ExPASy, EBI, Israel, Japan] Wang Y.-P., Birkenhead K., Boesten B., Manian S., O'Gara F.; "Genetic analysis and regulation of the Rhizobium meliloti genes controlling C4-dicarboxylic acid transport."; Gene 85:135-144(1989).

Comments

FUNCTION: Member of the two-component regulatory system dctB/dctD involved in the transport of C4-dicarboxylates. DctB functions as a membrane-associated protein kinase that phosphorylates dctD in response to environmental signals.
CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
SIMILARITY: Contains 1 histidine kinase domain.
SEQUENCE CAUTION:
- Sequence=M33555; Type=Frameshift; Positions=20, 161;

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

J03683; AAA63511.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J03683; AAA63510.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J03683; AAA63512.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M26531; AAA26249.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL591985; CAC49924.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M26399; AAA26251.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M33555; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]

PIR

B33586; B33586.
D96032; D96032.

RefSeq

NP_438064.1; -.

3D structure databases

HSSP

P02933; 1BXD. [HSSP ENTRY / PDB]

ModBase

P13633.

Enzyme and pathway databases

BioCyc

SMEL266834:SMB20612-MON; -.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0000155;	Molecular function: two-component sensor activity (inferred from electronic annotation from InterPro).
GO:0018106;	Biological process: peptidyl-histidine phosphorylation (inferred from electronic annotation from InterPro).
GO:0000160;	Biological process: two-component signal transduction system (phosphorelay) (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR003594; ATP_bd_ATPase.
IPR004358; Sig_transdc_His_kin-like_C.
IPR003661; Sig_transdc_His_kin_sub1_dim/P.
IPR005467; Sig_transdc_His_kinase_core.
IPR017055; Sig_transdc_His_kinase_DctB.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.565.10; ATP_bd_ATPase; 1.

Pfam

PF02518; HATPase_c; 1.
PF00512; HisKA; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF036431; STHK_DctB; 1.

PRINTS

PR00344; BCTRLSENSOR.

SMART

SM00387; HATPase_c; 1.
SM00388; HisKA; 1.
SMART graphical view of domain structure.

PROSITE

PS50109; HIS_KIN; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P13633.

Genome annotation databases

1237856; -.

AL591985_GR; RB1524.

sme:SMb20612; -.

fig|266834.1.peg.6159; -.

Phylogenomic databases

HOGENOM

P13633; -.

Genome annotation databases

CMR

P13633; RB1524.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cell inner membrane; Cell membrane; Complete proteome; Kinase; Membrane; Phosphoprotein; Plasmid; Transferase; Transmembrane; Two-component regulatory system.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 621`	`621`	`C4-dicarboxylate transport sensor protein dctB.`	`PRO_0000074748`
`TOPO_DOM`	`1 26`	`26`	`Cytoplasmic (Potential).`
`TRANSMEM`	`27 45`	`19`	`Potential.`
`TOPO_DOM`	`46 320`	`275`	`Periplasmic.`
`TRANSMEM`	`321 338`	`18`	`Potential.`
`TOPO_DOM`	`339 621`	`283`	`Cytoplasmic (Potential).`
`DOMAIN`	`412 621`	`210`	`Histidine kinase.`
`MOD_RES`	`415 415`		`Phosphohistidine; by autocatalysis (By similarity).`
`CONFLICT`	`3 3`		`H -> N (in Ref. 1 and 5).`
`CONFLICT`	`102 102`		`P -> Q (in Ref. 1; AAA63511/AAA63510).`
`CONFLICT`	`174 174`		`N -> K (in Ref. 5).`
`CONFLICT`	`504 504`		`L -> I (in Ref. 1; AAA63511/AAA63510).`
`CONFLICT`	`540 540`		`D -> N (in Ref. 1; AAA63511/AAA63510).`
`CONFLICT`	`548 551`		`EEAA -> KAAP (in Ref. 1; AAA63511/AAA63510).`
`CONFLICT`	`615 615`		`A -> T (in Ref. 1; AAA63511/AAA63510).`

Sequence information

Length: 621 AA [This is the length of the unprocessed precursor]

Molecular weight: 67133 Da [This is the MW of the unprocessed precursor]

CRC64: D60F724E2CA6BCC7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MHHVRMVKLP AEASDPHALR SRARRSWLVF AAVALVLLAA GLLLARDYGR SQALAGLAGQ 

        70         80         90        100        110        120 
SRIDASLKAS LLRAVVERQR ALPLVLADDA AIRGALLSPD RPSLDRINRK LEALATSAEA 

       130        140        150        160        170        180 
AVIYLIDRSG VAVAASNWQE PTSFVGNDYA FRDYFRLAVR DGMAEHFAMG TVSNRPGLYI 

       190        200        210        220        230        240 
SRRVDGPGGP LGVIVAKLEF DGVEADWQAS GKPAYVTDRR GIVLITSLPS WRFMTTKPIA 

       250        260        270        280        290        300 
EDRLAPIRES LQFGDAPLLP LPFRKIEARP DGSSTLDALL PGDSTAAFLR VETMVPSTNW 

       310        320        330        340        350        360 
RLEQLSPLKA PLAAGAREAQ LLTLAALVPL LALAALLLRR RQVVAMRSAE ERLARNALEA 

       370        380        390        400        410        420 
SVEERTRDLR MARDRLETEI ADHRQTTEKL QAVQQDLVQA NRLAILGQVA AGVAHEINQP 

       430        440        450        460        470        480 
VATIRAYADN ARTFLHRGQT VTAAENMESI AELTERVGAI TDELRRFARK GHFAAGPTAM 

       490        500        510        520        530        540 
KEVVEGALML LRSRFAGRMD AIRLDLPPDG LQALGNRIRL EQVLINLLQN ALEAIGDSED 

       550        560        570        580        590        600 
GAIQVRCEEA AGGIALTVAD NGPGIAADVR EELFTPFNTS KEDGLGLGLA ISKEIVSDYG 

       610        620 
GTIEVESGPS GTTFAVNLKK A

P13633 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools