ID   DPPD_LACLM              Reviewed;         349 AA.
AC   A2RI77;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Dipeptide transport ATP-binding protein DppD {ECO:0000305};
DE            EC=7.4.2.9 {ECO:0000305|PubMed:11409543};
GN   Name=dppD {ECO:0000303|PubMed:11409543};
GN   OrderedLocusNames=llmg_0366 {ECO:0000312|EMBL:CAL96971.1};
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RC   STRAIN=MG1363;
RX   PubMed=11409543; DOI=10.1007/s002030100270;
RA   Sanz Y., Lanfermeijer F.C., Renault P., Bolotin A., Konings W.N.,
RA   Poolman B.;
RT   "Genetic and functional characterization of dpp genes encoding a dipeptide
RT   transport system in Lactococcus lactis.";
RL   Arch. Microbiol. 175:334-343(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
CC   -!- FUNCTION: Part of the ABC transporter DppABCDF involved in dipeptide
CC       transport (PubMed:11409543). Responsible for energy coupling to the
CC       transport system (Probable). {ECO:0000269|PubMed:11409543,
CC       ECO:0000305}.
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:0000305|PubMed:11409543};
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:0000305|PubMed:11409543}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; AM406671; CAL96971.1; -; Genomic_DNA.
DR   RefSeq; WP_011834423.1; NZ_WJVF01000001.1.
DR   AlphaFoldDB; A2RI77; -.
DR   SMR; A2RI77; -.
DR   STRING; 416870.llmg_0366; -.
DR   EnsemblBacteria; CAL96971; CAL96971; llmg_0366.
DR   GeneID; 61108670; -.
DR   KEGG; llm:llmg_0366; -.
DR   eggNOG; COG0444; Bacteria.
DR   HOGENOM; CLU_000604_1_23_9; -.
DR   OMA; YEPAHPY; -.
DR   PhylomeDB; A2RI77; -.
DR   BioCyc; LLAC416870:LLMG_RS01885-MON; -.
DR   Proteomes; UP000000364; 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; 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; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW   Peptide transport; Protein transport; Translocase; Transport.
FT   CHAIN           1..349
FT                   /note="Dipeptide transport ATP-binding protein DppD"
FT                   /id="PRO_0000452198"
FT   DOMAIN          7..258
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         43..50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   349 AA;  38910 MW;  B45B8E923F545B15 CRC64;
     MAEEKVLEVK NLHVNFHTYA GDVKAIRNVS FDLEKGQTLA IVGESGSGKS VTTKTLMGLN
     AKNAEIPEGE LLFKGRNLLD LKEEEWQKIR GNEISMIFQD PMTSLDPTMR IGKQIAEPLL
     KHNKGMSKAD AMKRALELMQ QVGIPDAEVH INDYPHQWSG GMRQRAVIAI ALAADPEILI
     ADEPTTALDV TIQAQIMHMM AELQERINSS IVFITHDLGV VAGFAHKVAV MYAGEIVEYG
     TVEEIFYNPQ HPYTWGLLDS MPTVDSSVDR LVSIPGTPPD LLNPPKGDAF AARNKFALAI
     DFEEEPPYFE VSPTHFAKTW LLDPRAPKVT PSDNILARWK RWEELKGDK