DDPF_ECOLI
ID DDPF_ECOLI Reviewed; 308 AA.
AC P77622; P76870;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Probable D,D-dipeptide transport ATP-binding protein DdpF;
GN Name=ddpF {ECO:0000303|PubMed:10500118}; Synonyms=yddO;
GN OrderedLocusNames=b1483, JW1478;
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 (PubMed:9097039). Probably
CC responsible for energy coupling to the transport system.
CC {ECO:0000305|PubMed:9097039}.
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: Cell inner membrane {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}.
CC -!- INDUCTION: Induced by RpoS in stationary phase.
CC {ECO:0000269|PubMed:9751644}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; U00096; AAC74556.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15138.1; -; Genomic_DNA.
DR PIR; F64901; F64901.
DR RefSeq; NP_416000.1; NC_000913.3.
DR RefSeq; WP_001285536.1; NZ_LN832404.1.
DR AlphaFoldDB; P77622; -.
DR SMR; P77622; -.
DR BioGRID; 4260961; 99.
DR ComplexPortal; CPX-4321; Dipeptide ABC transporter complex.
DR IntAct; P77622; 2.
DR STRING; 511145.b1483; -.
DR TCDB; 3.A.1.5.38; the atp-binding cassette (abc) superfamily.
DR PaxDb; P77622; -.
DR PRIDE; P77622; -.
DR EnsemblBacteria; AAC74556; AAC74556; b1483.
DR EnsemblBacteria; BAA15138; BAA15138; BAA15138.
DR GeneID; 946020; -.
DR KEGG; ecj:JW1478; -.
DR KEGG; eco:b1483; -.
DR PATRIC; fig|1411691.4.peg.784; -.
DR EchoBASE; EB3547; -.
DR eggNOG; COG4608; Bacteria.
DR HOGENOM; CLU_000604_1_23_6; -.
DR InParanoid; P77622; -.
DR OMA; VACHWAE; -.
DR PhylomeDB; P77622; -.
DR BioCyc; EcoCyc:YDDO-MON; -.
DR PRO; PR:P77622; -.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042938; P:dipeptide transport; IC:ComplexPortal.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR013563; Oligopep_ABC_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF08352; oligo_HPY; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01727; oligo_HPY; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Peptide transport; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..308
FT /note="Probable D,D-dipeptide transport ATP-binding protein
FT DdpF"
FT /id="PRO_0000093164"
FT DOMAIN 8..243
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 49..56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 308 AA; 34621 MW; E7E17DD361EC07BE CRC64;
MSDTLLTLRD VHINFPARKN WLGKTTEHVH AINGIDLQIR RGETLGIVGE SGCGKSTLAQ
LLMGMLQPSH GQYIRSGSQR IMQMVFQDPL SSLNPRLPVW RIITEPLWIA KRSSEQQRRA
LAEELAVQVG IRPEYLDRLP HAFSGGQRQR IAIARALSSQ PDVIVLDEPT SALDISVQAQ
ILNLLVTLQE NHGLTYVLIS HNVSVIRHMS DRVAVMYLGQ IVELGDAQQV LTAPAHPYTR
LLLDSLPAID KPLEEEWALR KTDLPGNRTL PQGCFFYERC PLATHGCEVR QSLAIREDGR
ELRCWRAL
