ID   DPPC_PSEAB              Reviewed;         303 AA.
AC   A0A0H2ZFV0;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Di/tripeptide transport system permease protein DppC {ECO:0000305};
GN   Name=dppC {ECO:0000303|PubMed:25338022};
GN   OrderedLocusNames=PA14_58450 {ECO:0000312|EMBL:ABJ13771.1};
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 the
CC       translocation of the substrate across the membrane (Probable).
CC       {ECO:0000269|PubMed:25338022, ECO:0000305}.
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
CC       {ECO:0000250|UniProtKB:P0AEG1}; Multi-pass membrane protein
CC       {ECO:0000255}.
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 binding-protein-dependent transport system
CC       permease family. OppBC subfamily. {ECO:0000305}.
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DR   EMBL; CP000438; ABJ13771.1; -; Genomic_DNA.
DR   RefSeq; WP_003094448.1; NZ_CP034244.1.
DR   AlphaFoldDB; A0A0H2ZFV0; -.
DR   EnsemblBacteria; ABJ13771; ABJ13771; PA14_58450.
DR   KEGG; pau:PA14_58450; -.
DR   HOGENOM; CLU_028518_1_1_6; -.
DR   OMA; RAWWVVS; -.
DR   BioCyc; PAER208963:G1G74-4923-MON; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015833; P:peptide transport; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   CDD; cd06261; TM_PBP2; 1.
DR   Gene3D; 1.10.3720.10; -; 1.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   InterPro; IPR025966; OppC_N.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   Pfam; PF12911; OppC_N; 1.
DR   SUPFAM; SSF161098; SSF161098; 1.
DR   PROSITE; PS50928; ABC_TM1; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Membrane; Peptide transport;
KW   Protein transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..303
FT                   /note="Di/tripeptide transport system permease protein
FT                   DppC"
FT                   /id="PRO_0000452196"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          99..288
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   SEQUENCE   303 AA;  32363 MW;  FC173799C45A4181 CRC64;
     MNAMHNAPAS DPSLVYPSPL KEFWQSFAHN KGALGGLLFM LLIVFCALFA PWVAPYDPSE
     QFRDFLLTPP SWLEGGQARF LLGTDELGRD LLSRLIHGAR LSLLIGLSSV VISLIPGILL
     GLLAGFSPNR AGPLIMRLMD IMLALPSLLL AVAIVAILGP GLINTVIAIA IVSLPAYVRL
     TRAAVMTELN RDYVTASRLA GAGTLRLMFV CVLPNCMAPL IVQATLSFSS AILDAAALGF
     LGLGVQPPTP EWGTMLASAR DYIERAWWVV SLPGLTILLS VLAINLMGDG LRDALDPKLK
     NAA