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 15-MAR-2017, entry version 128. 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., RA Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., RA Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., RA Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., RA Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.; RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome RT corresponding to 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., RA Mau B., 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 RT MG1655 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., RA Hutchins C., 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: RT attributes of catalytic efficiency, stereoselectivity and regulation RT with implications 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, RT immunity, or 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 CC for the translocation of the substrate across the membrane. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (DdpD CC and DdpF), two transmembrane proteins (DdpB and DdpC) and a CC solute-binding protein (DdpA). {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane CC protein. CC -!- INDUCTION: Induced by RpoS in stationary phase. CC {ECO:0000269|PubMed:9751644}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. OppBC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_LN832404.1. DR ProteinModelPortal; P77308; -. DR BioGrid; 4260211; 201. 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; 32118266; VBIEscCol129921_1553. DR EchoBASE; EB3550; -. DR EcoGene; EG13789; ddpB. DR eggNOG; ENOG4105CJM; Bacteria. DR eggNOG; COG0601; LUCA. DR HOGENOM; HOG000170242; -. DR InParanoid; P77308; -. DR KO; K02033; -. DR OMA; AAWKHGT; -. DR PhylomeDB; P77308; -. DR BioCyc; EcoCyc:YDDR-MONOMER; -. DR PRO; PR:P77308; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc. DR GO; GO:0015833; P:peptide transport; IEA:UniProtKB-KW. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR CDD; cd06261; TM_PBP2; 1. DR Gene3D; 1.10.3720.10; -; 2. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 2. DR PROSITE; PS50928; ABC_TM1; 1. PE 1: Evidence at protein level; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Peptide transport; Protein transport; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 340 Probable D,D-dipeptide transport system FT permease protein DdpB. FT /FTId=PRO_0000060246. FT TOPO_DOM 1 11 Periplasmic. {ECO:0000255}. FT TRANSMEM 12 32 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 33 104 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 105 125 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 126 135 Periplasmic. {ECO:0000255}. FT TRANSMEM 136 156 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 157 199 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 200 220 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 221 246 Periplasmic. {ECO:0000255}. FT TRANSMEM 247 269 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 270 279 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 280 300 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 301 301 Periplasmic. {ECO:0000255}. FT TRANSMEM 302 322 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 323 340 Cytoplasmic. {ECO:0000255}. FT DOMAIN 97 327 ABC transmembrane type-1. FT {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 //