ID   DPPD_PSEAB              Reviewed;         324 AA.
AC   A0A0H2ZGN6;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=Di/tripeptide transport ATP-binding protein DppD {ECO:0000305};
DE            EC=7.4.2.9 {ECO:0000250|UniProtKB:P0AAG0};
GN   Name=dppD {ECO:0000303|PubMed:25338022};
GN   OrderedLocusNames=PA14_58470 {ECO:0000312|EMBL:ABJ13772.1};
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; ABJ13772.1; -; Genomic_DNA.
DR   RefSeq; WP_003094451.1; NZ_CP034244.1.
DR   AlphaFoldDB; A0A0H2ZGN6; -.
DR   SMR; A0A0H2ZGN6; -.
DR   EnsemblBacteria; ABJ13772; ABJ13772; PA14_58470.
DR   KEGG; pau:PA14_58470; -.
DR   HOGENOM; CLU_000604_1_23_6; -.
DR   OMA; MSSLNPC; -.
DR   BioCyc; PAER208963:G1G74-4924-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..324
FT                   /note="Di/tripeptide transport ATP-binding protein DppD"
FT                   /id="PRO_0000452199"
FT   DOMAIN          4..253
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         39..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   324 AA;  35399 MW;  C160B81E22B73F57 CRC64;
     MSLLDIKNLS VRFGDTTAVP VVDGLDLSVD KGEVLAIVGE SGSGKSVTMM ALMGLIDAPG
     WVSADHLRFD GHDMLTLKGR QRRRIVGKDM AMVFQDPMTA LNPSYTVGYQ IEEVLRLHLG
     LRGKALRQRA LELLERVEIP AAASRLDAYP HQLSGGMSQR VAIAMAIAAE PKLLIADEPT
     TALDVTIQAQ IMELLLNLQR DQDMALILIT HDLAVVAETA QRVCVMYAGE AVEIGGVPAL
     FDRPTHPYTE ALIKAIPEHC AGEARLATLP GIVPGRYDRP RGCLLSPRCP YAQEHCRQER
     PALEAHERGA VRCFYPLNLL NEVA