DPPA2_PSEAB
ID DPPA2_PSEAB Reviewed; 532 AA.
AC A0A0H2ZGW2;
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 2 {ECO:0000305};
DE Flags: Precursor;
GN Name=dppA2 {ECO:0000303|PubMed:25338022};
GN OrderedLocusNames=PA14_58360 {ECO:0000312|EMBL:ABJ13765.1};
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). Shows high flexibility on
CC substrate recognition. Efficiently uses tripeptides (PubMed:25338022).
CC {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 (DppA2) (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; ABJ13765.1; -; Genomic_DNA.
DR RefSeq; WP_003141332.1; NZ_CP034244.1.
DR AlphaFoldDB; A0A0H2ZGW2; -.
DR SMR; A0A0H2ZGW2; -.
DR EnsemblBacteria; ABJ13765; ABJ13765; PA14_58360.
DR KEGG; pau:PA14_58360; -.
DR HOGENOM; CLU_017028_7_0_6; -.
DR OMA; YIPLTYQ; -.
DR BioCyc; PAER208963:G1G74-4915-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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..532
FT /note="Di/tripeptide-binding protein 2"
FT /id="PRO_0000452189"
SQ SEQUENCE 532 AA; 59467 MW; FABCCAAD682331FB CRC64;
MRPRSALRYS LLLLAFAASA AIQAQPKTLA VCTEAAPEGF DPARYTSGYT FDASAHPLYN
ALAAFAPGSA TVIPALAESW DVSADGLVYT FRLRQGVKFH STDYFKPSRE FNADDVLFSF
QRMLDPQHPA HDLSPSGYPY ADAMQLRDII ERIEKIDEHQ VRFVLKHPEA PFLADLAMPF
GSILSAEYAG QLIARGKGDE LNSKPIGTGP FVFTRYRKDA QVRYAANPDY WKGKPAIDHL
VLAITLDPNV RVQRLRRNEC QIALTPKPED VAALRQDPQL TVLEEAAMIT SHAAINTRHE
PFDDPRVRRA IAMGFNKSSY LKIVFGDQAR PAIGPYPPML LGYDDSIRDW PYDPERAKAL
LKEAGVAPDT PLNLYISTGS GPGGNPARVA QLIQSDLAAI GIRVNIHQFE WGEMVKRTKA
GEHDMMLYSW IGDNGDPDNF LTHNLGCASV ESGENRARWC DKGFDEAIRK ARMSNDESQR
VALYKEAQRI FHEQMPWLPL AHPLMFDAQR KNVSGYRMSP MSARDFSRVK LD