DDPC_ECOLI
ID DDPC_ECOLI Reviewed; 298 AA.
AC P77463;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Probable D,D-dipeptide transport system permease protein DdpC;
GN Name=ddpC; Synonyms=yddQ; OrderedLocusNames=b1485, JW1480;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP INDUCTION.
RX PubMed=9751644; DOI=10.1016/s1074-5521(98)90005-9;
RA Lessard I.A.D., Pratt S.D., McCafferty D.G., Bussiere D.E., Hutchins C.,
RA Wanner B.L., Katz L., Walsh C.T.;
RT "Homologs of the vancomycin resistance D-Ala-D-Ala dipeptidase VanX in
RT Streptomyces toyocaensis, Escherichia coli and Synechocystis: attributes of
RT catalytic efficiency, stereoselectivity and regulation with implications
RT for function.";
RL Chem. Biol. 5:489-504(1998).
RN [5]
RP GENE NAME.
RX PubMed=10500118; DOI=10.1073/pnas.96.20.11028;
RA Lessard I.A.D., Walsh C.T.;
RT "VanX, a bacterial D-alanyl-D-alanine dipeptidase: resistance, immunity, or
RT survival function?";
RL Proc. Natl. Acad. Sci. U.S.A. 96:11028-11032(1999).
RN [6]
RP TOPOLOGY.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=11867724; DOI=10.1073/pnas.052018199;
RA Drew D., Sjoestrand D., Nilsson J., Urbig T., Chin C.-N., de Gier J.-W.,
RA von Heijne G.;
RT "Rapid topology mapping of Escherichia coli inner-membrane proteins by
RT prediction and PhoA/GFP fusion analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2690-2695(2002).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Part of the ABC transporter complex DdpABCDF, which is
CC probably involved in D,D-dipeptide transport. Probably responsible for
CC the translocation of the substrate across the membrane.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (DdpD and
CC DdpF), two transmembrane proteins (DdpB and DdpC) and a solute-binding
CC protein (DdpA). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- INDUCTION: Induced by RpoS in stationary phase.
CC {ECO:0000269|PubMed:9751644}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. OppBC subfamily. {ECO:0000305}.
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DR EMBL; U00096; AAC74558.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15140.1; -; Genomic_DNA.
DR PIR; H64901; H64901.
DR RefSeq; NP_416002.1; NC_000913.3.
DR RefSeq; WP_000979626.1; NZ_SSZK01000038.1.
DR AlphaFoldDB; P77463; -.
DR BioGRID; 4260963; 273.
DR ComplexPortal; CPX-4321; Dipeptide ABC transporter complex.
DR IntAct; P77463; 2.
DR STRING; 511145.b1485; -.
DR TCDB; 3.A.1.5.38; the atp-binding cassette (abc) superfamily.
DR PaxDb; P77463; -.
DR PRIDE; P77463; -.
DR EnsemblBacteria; AAC74558; AAC74558; b1485.
DR EnsemblBacteria; BAA15140; BAA15140; BAA15140.
DR GeneID; 946028; -.
DR KEGG; ecj:JW1480; -.
DR KEGG; eco:b1485; -.
DR PATRIC; fig|1411691.4.peg.782; -.
DR EchoBASE; EB3549; -.
DR eggNOG; COG1173; Bacteria.
DR HOGENOM; CLU_028518_1_1_6; -.
DR InParanoid; P77463; -.
DR OMA; FIRSVYI; -.
DR PhylomeDB; P77463; -.
DR BioCyc; EcoCyc:YDDQ-MON; -.
DR PRO; PR:P77463; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoliWiki.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042938; P:dipeptide transport; IC:ComplexPortal.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR InterPro; IPR025966; OppC_N.
DR Pfam; PF00528; BPD_transp_1; 1.
DR Pfam; PF12911; OppC_N; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Peptide transport;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..298
FT /note="Probable D,D-dipeptide transport system permease
FT protein DdpC"
FT /id="PRO_0000060245"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 55..96
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 118..124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 167..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 239..260
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 282..298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 97..282
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 298 AA; 31971 MW; 721AB0225634AF6F CRC64;
MMLSEETSAV RPQKQTRFNG AKLVWMLKGS PLTVTSAVII VLMLLMMIFS PWLATHDPNA
IDLTARLLPP SAAHWFGTDE VGRDLFSRVL VGSQQSILAG LVVVAIAGMI GSLLGCLSGV
LGGRADAIIM RIMDIMLSIP SLVLTMALAA ALGPSLFNAM LAIAIVRIPF YVRLARGQAL
VVRQYTYVQA AKTFGASRWH LINWHILRNS LPPLIVQASL DIGSAILMAA TLGFIGLGAQ
QPSAEWGAMV ANGRNYVLDQ WWYCAFPGAA ILLTAVGFNL FGDGIRDLLD PKAGGKQS
