DDPA_ECOLI
ID DDPA_ECOLI Reviewed; 516 AA.
AC P76128; P76874; P77769;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Probable D,D-dipeptide-binding periplasmic protein DdpA;
DE Flags: Precursor;
GN Name=ddpA; Synonyms=yddS; OrderedLocusNames=b1487, JW5240;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP INDUCTION.
RX PubMed=9751644; DOI=10.1016/s1074-5521(98)90005-9;
RA Lessard I.A.D., Pratt S.D., McCafferty D.G., Bussiere D.E., Hutchins C.,
RA Wanner B.L., Katz L., Walsh C.T.;
RT "Homologs of the vancomycin resistance D-Ala-D-Ala dipeptidase VanX in
RT Streptomyces toyocaensis, Escherichia coli and Synechocystis: attributes of
RT catalytic efficiency, stereoselectivity and regulation with implications
RT for function.";
RL Chem. Biol. 5:489-504(1998).
RN [5]
RP GENE NAME.
RX PubMed=10500118; DOI=10.1073/pnas.96.20.11028;
RA Lessard I.A.D., Walsh C.T.;
RT "VanX, a bacterial D-alanyl-D-alanine dipeptidase: resistance, immunity, or
RT survival function?";
RL Proc. Natl. Acad. Sci. U.S.A. 96:11028-11032(1999).
CC -!- FUNCTION: Part of the ABC transporter complex DdpABCDF, which is
CC probably involved in D,D-dipeptide transport.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (DdpD and
CC DdpF), two transmembrane proteins (DdpB and DdpC) and a solute-binding
CC protein (DdpA). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- INDUCTION: Induced by RpoS in stationary phase.
CC {ECO:0000269|PubMed:9751644}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.
CC {ECO:0000305}.
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DR EMBL; U00096; AAC74560.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15142.2; -; Genomic_DNA.
DR PIR; B64902; B64902.
DR RefSeq; NP_416004.1; NC_000913.3.
DR RefSeq; WP_000830550.1; NZ_SSZK01000038.1.
DR AlphaFoldDB; P76128; -.
DR SMR; P76128; -.
DR BioGRID; 4261978; 368.
DR ComplexPortal; CPX-4321; Dipeptide ABC transporter complex.
DR DIP; DIP-11672N; -.
DR IntAct; P76128; 2.
DR STRING; 511145.b1487; -.
DR TCDB; 3.A.1.5.38; the atp-binding cassette (abc) superfamily.
DR jPOST; P76128; -.
DR PaxDb; P76128; -.
DR PRIDE; P76128; -.
DR EnsemblBacteria; AAC74560; AAC74560; b1487.
DR EnsemblBacteria; BAA15142; BAA15142; BAA15142.
DR GeneID; 946052; -.
DR KEGG; ecj:JW5240; -.
DR KEGG; eco:b1487; -.
DR PATRIC; fig|1411691.4.peg.780; -.
DR EchoBASE; EB3551; -.
DR eggNOG; COG0747; Bacteria.
DR HOGENOM; CLU_017028_7_4_6; -.
DR InParanoid; P76128; -.
DR OMA; AGPHVWF; -.
DR PhylomeDB; P76128; -.
DR BioCyc; EcoCyc:YDDS-MON; -.
DR PRO; PR:P76128; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:1904680; F:peptide transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042938; P:dipeptide transport; IC:ComplexPortal.
DR GO; GO:0015833; P:peptide transport; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR030678; Peptide/Ni-bd.
DR InterPro; IPR039424; SBP_5.
DR InterPro; IPR023765; SBP_5_CS.
DR InterPro; IPR000914; SBP_5_dom.
DR PANTHER; PTHR30290; PTHR30290; 1.
DR Pfam; PF00496; SBP_bac_5; 1.
DR PIRSF; PIRSF002741; MppA; 1.
DR PROSITE; PS01040; SBP_BACTERIAL_5; 1.
PE 2: Evidence at transcript level;
KW Peptide transport; Periplasm; Protein transport; Reference proteome;
KW Signal; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..516
FT /note="Probable D,D-dipeptide-binding periplasmic protein
FT DdpA"
FT /id="PRO_0000031805"
SQ SEQUENCE 516 AA; 57641 MW; 86E1C32CC3E06FB9 CRC64;
MKRSISFRPT LLALVLATNF PVAHAAVPKD MLVIGKAADP QTLDPAVTID NNDWTVTYPS
YQRLVQYKTD GDKGSTDVEG DLASSWKASD DQKEWTFTLK DNAKFADGTP VTAEAVKLSF
ERLLKIGQGP AEAFPKDLKI DAPDEHTVKF TLSQPFAPFL YTLANDGASI INPAVLKEHA
ADDARGFLAQ NTAGSGPFML KSWQKGQQLV LVPNPHYPGN KPNFKRVSVK IIGESASRRL
QLSRGDIDIA DALPVDQLNA LKQENKVNVA EYPSLRVTYL YLNNSKAPLN QADLRRAISW
STDYQGMVNG ILSGNGKQMR GPIPEGMWGY DATAMQYNHD ETKAKAEWDK VTSKPTSLTF
LYSDNDPNWE PIALATQSSL NKLGIIVKLE KLANATMRDR VGKGDYDIAI GNWSPDFADP
YMFMNYWFES DKKGLPGNRS FYENSEVDKL LRNALATTDQ TQRTRDYQQA QKIVIDDAAY
VYLFQKNYQL AMNKEVKGFV FNPMLEQVFN INTMSK