DPPA4_PSEAB
ID DPPA4_PSEAB Reviewed; 533 AA.
AC A0A0H2ZGV7;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Di/tripeptide-binding protein 4 {ECO:0000305};
DE Flags: Precursor;
GN Name=dppA4 {ECO:0000303|PubMed:25338022};
GN OrderedLocusNames=PA14_58420 {ECO:0000312|EMBL:ABJ13769.1};
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, AND SUBUNIT.
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). Prefers dipeptides with
CC acidic residues at the C-terminal end. Efficiently uses tripeptides
CC (PubMed:25338022). {ECO:0000269|PubMed:25338022}.
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 (DppA4) (PubMed:25338022). Five orthologous SBPs (DppA1-A5) are
CC present in P.aeruginosa, which increases the substrate specificity of
CC the DppBCDF transporter (PubMed:25338022).
CC {ECO:0000269|PubMed:25338022}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.
CC {ECO:0000305}.
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DR EMBL; CP000438; ABJ13769.1; -; Genomic_DNA.
DR RefSeq; WP_003141337.1; NZ_CP034244.1.
DR AlphaFoldDB; A0A0H2ZGV7; -.
DR SMR; A0A0H2ZGV7; -.
DR EnsemblBacteria; ABJ13769; ABJ13769; PA14_58420.
DR KEGG; pau:PA14_58420; -.
DR HOGENOM; CLU_017028_7_0_6; -.
DR OMA; KESPWVP; -.
DR BioCyc; PAER208963:G1G74-4921-MON; -.
DR Proteomes; UP000000653; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:UniProt.
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 InterPro; IPR030678; Peptide/Ni-bd.
DR InterPro; IPR039424; SBP_5.
DR InterPro; IPR000914; SBP_5_dom.
DR PANTHER; PTHR30290; PTHR30290; 1.
DR Pfam; PF00496; SBP_bac_5; 1.
DR PIRSF; PIRSF002741; MppA; 1.
PE 1: Evidence at protein level;
KW Peptide transport; Protein transport; Signal; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..533
FT /note="Di/tripeptide-binding protein 4"
FT /id="PRO_0000452191"
SQ SEQUENCE 533 AA; 58811 MW; D148727D2CA0E5F1 CRC64;
MLHPLLRHLP LALALALCAA GAAQAKNLVV CTEASPEGFD IVQYTGAVTA DASAETVFNR
LLAFRPGTTE VIPGLAERWD VSADGLSYTF HLRPGVKFHT TDYFKPTRSL NADDVLWTFQ
RALDPKHPWH ASALRGYAYF DAMGMGELIK SVEKVDELTV RFVLNRPEAP FLRDMAMPFA
SIYSAEYGDQ LLAAGKQGQL NNQPIGTGPF VFKRYAKDAQ VRYTANPDYY AGKPPIDNLV
FAITLDPNVR MQKVRAGECQ VSLYPKPEDV PRLKQDPNLA VDEIDALLTT YIAINTQHKP
LDDPRVRQAI NLALDKKAML DAVFGPGAAS PAVGPYPPTL LGYNHSIQDW PHDPERARAL
LKEAGAENLR ITLFIRNGTS PTIPNPALAA QMLQADLAKA GIQLTIRSLE WGELLKRSKA
GEHDLSLLGW AGDNGDPDNF LSPNLSCAAA ESGENQARWC DKDFEALMRK AREVSDPAER
AKLYEQAQVV FHEQAPWIPL AYPKLFNVRR NTVQGYVINP LSNNNFATTS VKP