DDPD_ECOLI
ID DDPD_ECOLI Reviewed; 328 AA.
AC P77268;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Probable D,D-dipeptide transport ATP-binding protein DdpD;
GN Name=ddpD {ECO:0000303|PubMed:10500118}; Synonyms=yddP;
GN OrderedLocusNames=b1484, JW1479;
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).
CC -!- FUNCTION: Part of the ABC transporter complex DdpABCDF, which is
CC probably involved in D,D-dipeptide transport (PubMed:9097039). Probably
CC responsible for energy coupling to the transport system.
CC {ECO:0000305|PubMed:9097039}.
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 {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}.
CC -!- INDUCTION: Induced by RpoS in stationary phase.
CC {ECO:0000269|PubMed:9751644}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; U00096; AAC74557.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15139.1; -; Genomic_DNA.
DR PIR; G64901; G64901.
DR RefSeq; NP_416001.1; NC_000913.3.
DR RefSeq; WP_000193547.1; NZ_SSZK01000038.1.
DR AlphaFoldDB; P77268; -.
DR SMR; P77268; -.
DR BioGRID; 4260962; 121.
DR ComplexPortal; CPX-4321; Dipeptide ABC transporter complex.
DR DIP; DIP-11669N; -.
DR IntAct; P77268; 9.
DR STRING; 511145.b1484; -.
DR TCDB; 3.A.1.5.38; the atp-binding cassette (abc) superfamily.
DR PaxDb; P77268; -.
DR PRIDE; P77268; -.
DR EnsemblBacteria; AAC74557; AAC74557; b1484.
DR EnsemblBacteria; BAA15139; BAA15139; BAA15139.
DR GeneID; 946002; -.
DR KEGG; ecj:JW1479; -.
DR KEGG; eco:b1484; -.
DR PATRIC; fig|1411691.4.peg.783; -.
DR EchoBASE; EB3548; -.
DR eggNOG; COG0444; Bacteria.
DR HOGENOM; CLU_000604_1_23_6; -.
DR InParanoid; P77268; -.
DR OMA; QMTEVII; -.
DR PhylomeDB; P77268; -.
DR BioCyc; EcoCyc:YDDP-MON; -.
DR PRO; PR:P77268; -.
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:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042938; P:dipeptide transport; IC:ComplexPortal.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR013563; Oligopep_ABC_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF08352; oligo_HPY; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01727; oligo_HPY; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Peptide transport; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..328
FT /note="Probable D,D-dipeptide transport ATP-binding protein
FT DdpD"
FT /id="PRO_0000093165"
FT DOMAIN 6..257
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 328 AA; 36100 MW; 76EAFDCAEFED5E6C CRC64;
MTQPVLDIQQ LHLSFPGFNG DVHALNNVSL QINRGEIVGL VGESGSGKSV TAMLIMRLLP
TGSYCVHRGQ ISLLGEDVLN AREKQLRQWR GARVAMIFQE PMTALNPTRR IGLQMMDVIR
HHQPISRREA RAKAIDLLEE MQIPDAVEVM SRYPFELSGG MRQRVMIALA FSCEPQLIIA
DEPTTALDVT VQLQVLRLLK HKARASGTAV LFISHDMAVV SQLCDSVYVM YAGSVIESGV
TADVIHHPRH PYTIGLLQCA PEHGVPRQLL PAIPGTVPNL THLPDGCAFR DRCYAAGAQC
ENVPALTACG DNNQRCACWY PQQEVISV
