DDPB_ECOLI
ID DDPB_ECOLI Reviewed; 340 AA.
AC P77308;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Probable D,D-dipeptide transport system permease protein DdpB;
GN Name=ddpB; Synonyms=yddR; OrderedLocusNames=b1486, JW1481;
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).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Part of the ABC transporter complex DdpABCDF, which is
CC probably involved in D,D-dipeptide transport. Probably responsible for
CC the translocation of the substrate across the membrane.
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; Multi-pass membrane protein.
CC -!- INDUCTION: Induced by RpoS in stationary phase.
CC {ECO:0000269|PubMed:9751644}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. OppBC subfamily. {ECO:0000305}.
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DR EMBL; U00096; AAC74559.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15141.1; -; Genomic_DNA.
DR PIR; A64902; A64902.
DR RefSeq; NP_416003.1; NC_000913.3.
DR RefSeq; WP_000145123.1; NZ_SSZK01000038.1.
DR AlphaFoldDB; P77308; -.
DR SMR; P77308; -.
DR BioGRID; 4260211; 201.
DR BioGRID; 850405; 1.
DR ComplexPortal; CPX-4321; Dipeptide ABC transporter complex.
DR DIP; DIP-11671N; -.
DR IntAct; P77308; 2.
DR STRING; 511145.b1486; -.
DR TCDB; 3.A.1.5.38; the atp-binding cassette (abc) superfamily.
DR PaxDb; P77308; -.
DR PRIDE; P77308; -.
DR EnsemblBacteria; AAC74559; AAC74559; b1486.
DR EnsemblBacteria; BAA15141; BAA15141; BAA15141.
DR GeneID; 946044; -.
DR KEGG; ecj:JW1481; -.
DR KEGG; eco:b1486; -.
DR PATRIC; fig|1411691.4.peg.781; -.
DR EchoBASE; EB3550; -.
DR eggNOG; COG0601; Bacteria.
DR HOGENOM; CLU_036879_0_0_6; -.
DR InParanoid; P77308; -.
DR OMA; PDFWMGI; -.
DR PhylomeDB; P77308; -.
DR BioCyc; EcoCyc:YDDR-MON; -.
DR PRO; PR:P77308; -.
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:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042938; P:dipeptide transport; IC:ComplexPortal.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..340
FT /note="Probable D,D-dipeptide transport system permease
FT protein DdpB"
FT /id="PRO_0000060246"
FT TOPO_DOM 1..11
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 33..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 126..135
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 157..199
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 221..246
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..269
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 270..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 301
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 323..340
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 97..327
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 340 AA; 37345 MW; 5E684D9B0400487A CRC64;
MTFWSILRQR CWGLVLVVAG VCVITFIISH LIPGDPARLL AGDRASDAIV ENIRQQLGLD
QPLYVQFYRY VSDLFHGDLG TSIRTGRPVL EELRIFFPAT LELAFGALLL ALLIGIPLGI
LSAVWRNRWL DHLVRIMAIT GISTPAFWLG LGVIVLFYGH LQILPGGGRL DDWLDPPTHV
TGFYLLDALL EGNGEVFFNA LQHLILPALT LAFVHLGIVA RQIRSAMLEQ LSEDYIRTAR
ASGLPGWYIV LCYALPNALI PSITVLGLAL GDLLYGAVLT ETVFAWPGMG AWVVTSIQAL
DFPAVMGFAV VVSFAYVLVN LVVDLLYLWI DPRIGRGGGE
