ID   DPPF_LACLM              Reviewed;         312 AA.
AC   A2RI78; Q93QH3;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Dipeptide transport ATP-binding protein DppF {ECO:0000305};
DE            EC=7.4.2.9 {ECO:0000305|PubMed:11409543};
GN   Name=dppF {ECO:0000303|PubMed:11409543};
GN   OrderedLocusNames=llmg_0367 {ECO:0000312|EMBL:CAL96972.1};
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, SUBUNIT, AND DISRUPTION
RP   PHENOTYPE.
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   -!- DISRUPTION PHENOTYPE: Inactivation of the gene impairs growth on low
CC       concentrations of di-valine. {ECO:0000269|PubMed:11409543}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; AF247635; AAK58901.1; -; Genomic_DNA.
DR   EMBL; AM406671; CAL96972.1; -; Genomic_DNA.
DR   RefSeq; WP_011675407.1; NZ_WJVF01000001.1.
DR   AlphaFoldDB; A2RI78; -.
DR   SMR; A2RI78; -.
DR   STRING; 416870.llmg_0367; -.
DR   EnsemblBacteria; CAL96972; CAL96972; llmg_0367.
DR   GeneID; 61108671; -.
DR   KEGG; llm:llmg_0367; -.
DR   eggNOG; COG4608; Bacteria.
DR   HOGENOM; CLU_000604_1_23_9; -.
DR   OMA; EPLRTYY; -.
DR   PhylomeDB; A2RI78; -.
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:0022857; F:transmembrane transporter activity; IEA:UniProt.
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   PROSITE; PS00211; ABC_TRANSPORTER_1; 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..312
FT                   /note="Dipeptide transport ATP-binding protein DppF"
FT                   /id="PRO_0000452200"
FT   DOMAIN          10..255
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         45..52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   312 AA;  34883 MW;  6ACDE4D0177598E0 CRC64;
     MTEPKKVVEI KNLDLTFNKG KKGANKAINN VSLDIYEGET FGLVGESGSG KTTIGRAILK
     LYDNFITGGE ILFEGKDVRN LKGSELREYR SEAQMIFQDP QASLNGRMRV KDIVAEGLDA
     NGLVKTKAER DARVLELLRL VGLNDDHLTR YPHEFSGGQR QRIGIARALA VKPKFVVADE
     PISALDVSIQ AQVVNLMRDI QAKENLTYLF IAHDLSMVKY ISDRIGVMHW GKILEVGTSE
     QVYNHPIHPY TKSLLSSIPS PDPISERQRT PIVYDPTAEL DGQEREMREI TPGHFVFSTE
     AEAEVYKKNA TL