ID   DPPB_PSEAB              Reviewed;         336 AA.
AC   A0A0H2ZGW7;
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 DppB {ECO:0000305};
GN   Name=dppB {ECO:0000303|PubMed:25338022};
GN   OrderedLocusNames=PA14_58440 {ECO:0000312|EMBL:ABJ13770.1};
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:P0AEF8}; 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; ABJ13770.1; -; Genomic_DNA.
DR   RefSeq; WP_003105448.1; NZ_CP034244.1.
DR   AlphaFoldDB; A0A0H2ZGW7; -.
DR   SMR; A0A0H2ZGW7; -.
DR   EnsemblBacteria; ABJ13770; ABJ13770; PA14_58440.
DR   KEGG; pau:PA14_58440; -.
DR   HOGENOM; CLU_036879_0_0_6; -.
DR   OMA; WPGMGTF; -.
DR   BioCyc; PAER208963:G1G74-4922-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; IPR045621; BPD_transp_1_N.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   Pfam; PF19300; BPD_transp_1_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..336
FT                   /note="Di/tripeptide transport system permease protein
FT                   DppB"
FT                   /id="PRO_0000452194"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        307..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          96..325
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   SEQUENCE   336 AA;  37073 MW;  DDEADC2DF1740C0B CRC64;
     MLSFIARRLG LLIPTFFGVT LLTFALIRLI PGDPVEVMMG ERRVDPQMHA EALHRLGLDK
     PLYQQYLDYV GNLAQGNLGE SLTTREGVWH EFLTLFPATL ELSLAAMLFA GTFGLLAGVI
     AALKRGSLFD HGVMTVSLAG YSMPIFWWGL ILIMLFSVSL GWTPVSGRLD LLYDIEPKTG
     FMLIDTLLSD EQGSFLDAVR HLILPAIVLG TIPLAVIARM TRSAMLEVLR EDYVRTARAK
     GLSPARVVFV HALRNALIPV LTVFGLQVGT LLAGAVLTET IFSWPGIGKW LIDAISRRDY
     PVVQNGILLV ATLVILVNFV VDILYGLANP RIRHQR