ID   DPPD_ECO57              Reviewed;         327 AA.
AC   P0AAG1; P37314;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Dipeptide transport ATP-binding protein DppD {ECO:0000250|UniProtKB:P0AAG0};
DE            EC=7.4.2.9 {ECO:0000250|UniProtKB:P0AAG0};
GN   Name=dppD; OrderedLocusNames=Z4958, ECs4421;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Part of the ABC transporter DppABCDF involved in dipeptide
CC       transport. Responsible for energy coupling to the transport system.
CC       {ECO:0000250|UniProtKB:P0AAG0}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dipeptide(out) + ATP + H2O = a dipeptide(in) + ADP + H(+) +
CC         phosphate; Xref=Rhea:RHEA:23120, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:90799, ChEBI:CHEBI:456216; EC=7.4.2.9;
CC         Evidence={ECO:0000250|UniProtKB:P0AAG0};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (DppD and
CC       DppF), two transmembrane proteins (DppB and DppC) and a solute-binding
CC       protein (DppA). {ECO:0000250|UniProtKB:P0AAG0}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; AE005174; AAG58685.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37844.1; -; Genomic_DNA.
DR   PIR; A86028; A86028.
DR   PIR; E91181; E91181.
DR   RefSeq; NP_312448.1; NC_002695.1.
DR   RefSeq; WP_001196486.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0AAG1; -.
DR   SMR; P0AAG1; -.
DR   STRING; 155864.EDL933_4799; -.
DR   EnsemblBacteria; AAG58685; AAG58685; Z4958.
DR   EnsemblBacteria; BAB37844; BAB37844; ECs_4421.
DR   GeneID; 66672571; -.
DR   GeneID; 915714; -.
DR   KEGG; ece:Z4958; -.
DR   KEGG; ecs:ECs_4421; -.
DR   PATRIC; fig|386585.9.peg.4625; -.
DR   eggNOG; COG0444; Bacteria.
DR   HOGENOM; CLU_000604_1_23_6; -.
DR   OMA; GSMPRID; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015833; P:peptide transport; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Peptide transport; Protein transport;
KW   Reference proteome; Translocase; Transport.
FT   CHAIN           1..327
FT                   /note="Dipeptide transport ATP-binding protein DppD"
FT                   /id="PRO_0000092314"
FT   DOMAIN          4..254
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         40..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   327 AA;  35844 MW;  1CBFD72388EE0569 CRC64;
     MALLNVDKLS VHFGDESAPF RAVDRISYSV KQGEVVGIVG ESGSGKSVSS LAIMGLIDYP
     GRVMAEKLEF NGQDLQRISE KERRNLVGAE VAMIFQDPMT SLNPCYTVGF QIMEAIKVHQ
     GGNKSTRRQR AIDLLNQVGI PDPASRLDVY PHQLSGGMSQ RVMIAMAIAC RPKLLIADEP
     TTALDVTIQA QIIELLLELQ QKENMALVLI THDLALVAEA AHKIIVMYAG QVVETGDAHA
     IFHAPRHPYT QALLRALPEF AQDKERLASL PGVVPGKYDR PNGCLLNPRC PYATDRCRAE
     EPALNMLADG RQSKCHYPLD DAGRPTL