ID   DPPF_PSEAB              Reviewed;         323 AA.
AC   A0A0H2ZH52;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=Di/tripeptide transport ATP-binding protein DppF {ECO:0000305};
DE            EC=7.4.2.9 {ECO:0000250|UniProtKB:P0AAG0};
GN   Name=dppF {ECO:0000303|PubMed:25338022};
GN   OrderedLocusNames=PA14_58490 {ECO:0000312|EMBL:ABJ13773.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA   Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
RN   [2]
RP   FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC   STRAIN=UCBPP-PA14;
RX   PubMed=25338022; DOI=10.1371/journal.pone.0111311;
RA   Pletzer D., Lafon C., Braun Y., Koehler T., Page M.G., Mourez M.,
RA   Weingart H.;
RT   "High-throughput screening of dipeptide utilization mediated by the ABC
RT   transporter DppBCDF and its substrate-binding proteins DppA1-A5 in
RT   Pseudomonas aeruginosa.";
RL   PLoS ONE 9:e111311-e111311(2014).
CC   -!- FUNCTION: Part of the ABC transporter DppABCDF involved in the uptake
CC       of various di/tripeptides (PubMed:25338022). Is also involved in the
CC       uptake of phaseolotoxin, a toxic tripeptide inhibiting the enzyme
CC       ornithine carbamoyltransferase (PubMed:25338022). Responsible for
CC       energy coupling to the transport system (Probable).
CC       {ECO:0000269|PubMed:25338022, 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: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 (DppA1-A5) (PubMed:25338022). Five orthologous SBPs (DppA1-A5)
CC       are present in P.aeruginosa, which increases the substrate specificity
CC       of the DppBCDF transporter (PubMed:25338022).
CC       {ECO:0000269|PubMed:25338022}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral
CC       membrane protein {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the dppBCDF operon leads to reduced
CC       ability to utilize di/tripeptides as nitrogen source.
CC       {ECO:0000269|PubMed:25338022}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; CP000438; ABJ13773.1; -; Genomic_DNA.
DR   RefSeq; WP_003110330.1; NZ_CP034244.1.
DR   AlphaFoldDB; A0A0H2ZH52; -.
DR   SMR; A0A0H2ZH52; -.
DR   EnsemblBacteria; ABJ13773; ABJ13773; PA14_58490.
DR   KEGG; pau:PA14_58490; -.
DR   HOGENOM; CLU_000604_1_23_6; -.
DR   OMA; GRYPHMF; -.
DR   BioCyc; PAER208963:G1G74-4925-MON; -.
DR   Proteomes; UP000000653; 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   1: Evidence at protein level;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Peptide transport; Protein transport; Translocase;
KW   Transport.
FT   CHAIN           1..323
FT                   /note="Di/tripeptide transport ATP-binding protein DppF"
FT                   /id="PRO_0000452201"
FT   DOMAIN          5..254
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         47..54
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   323 AA;  36363 MW;  F33D8353012B0CD9 CRC64;
     METVLTARDL TRHYEVSRGL FKGHAQVRAL NGVSFELEAG KTLAVVGESG CGKSTLARAL
     TLIEEPTSGS LKIAGQEVKG ASKDQRRQLR RDVQMVFQNP YASLNPRQKI GDQLAEPLLI
     NTALSREERR EKVQQMMRQV GLRPEHYQRY PHMFSGGQRQ RIALARAMML QPKVLVADEP
     TSALDVSIQA QVLNLFMDLQ QQFRTAYVFI SHNLAVVRHV ADDVLVMYLG RPAEMGPADK
     LYENPLHPYT RALLSATPAI HPDPTKPKIR IQGELPNPLH PPEGCAFHKR CPYATERCRS
     EVPELRLLDQ RQVACHHAEQ FLG