ID LSRD_ECOLI Reviewed; 330 AA. AC P0AFS1; P76881; P77651; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 1. DT 02-SEP-2026, entry version 130. DE RecName: Full=Autoinducer 2 import system permease protein LsrD; DE Short=AI-2 import system permease protein LsrD; GN Name=lsrD; Synonyms=ydeZ; OrderedLocusNames=b1515, JW1508; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; 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 FUNCTION IN AI-2 IMPORT, AND INDUCTION. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=15601708; DOI=10.1128/jb.187.1.238-248.2005; RA Xavier K.B., Bassler B.L.; RT "Regulation of uptake and processing of the quorum-sensing autoinducer AI-2 RT in Escherichia coli."; RL J. Bacteriol. 187:238-248(2005). RN [5] RP INDUCTION. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=15743955; DOI=10.1128/jb.187.6.2066-2076.2005; RA Wang L., Hashimoto Y., Tsao C.-Y., Valdes J.J., Bentley W.E.; RT "Cyclic AMP (cAMP) and cAMP receptor protein influence both synthesis and RT uptake of extracellular autoinducer 2 in Escherichia coli."; RL J. Bacteriol. 187:2066-2076(2005). 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 LsrABCD involved in CC autoinducer 2 (AI-2) import. Probably responsible for the translocation CC of the substrate across the membrane (Probable). CC {ECO:0000305|PubMed:15601708}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (LsrA), CC two transmembrane proteins (LsrC and LsrD) and a solute-binding protein CC (LsrB). {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. CC -!- INDUCTION: In the absence of AI-2, repressed by LsrR. Induced by AI-2, CC via release of the LsrR repressor. In the absence of glucose, induced CC by cAMP-CRP by direct binding to the upstream region of the lsr CC promoter. {ECO:0000269|PubMed:15601708, ECO:0000269|PubMed:15743955}. CC -!- SIMILARITY: Belongs to the binding protein-dependent transport system CC permease family. AraH/RbsC 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; AAC74588.1; -; Genomic_DNA. DR EMBL; AP009048; BAA15202.1; -; Genomic_DNA. DR PIR; F64905; F64905. DR RefSeq; NP_416032.1; NC_000913.3. DR RefSeq; WP_001222721.1; NZ_CP009789.1. DR AlphaFoldDB; P0AFS1; -. DR BioGRID; 4259116; 6. DR ComplexPortal; CPX-4315; Autoinducer-2 ABC transporter complex. DR FunCoup; P0AFS1; 235. DR STRING; 511145.b1515; -. DR TCDB; 3.A.1.2.8; the atp-binding cassette (abc) superfamily. DR PaxDb; 511145-b1515; -. DR EnsemblBacteria; AAC74588; AAC74588; b1515. DR GeneID; 75202157; -. DR GeneID; 946264; -. DR KEGG; ecj:JW1508; -. DR KEGG; eco:b1515; -. DR KEGG; ecoc:C3026_08760; -. DR PATRIC; fig|1411691.4.peg.752; -. DR EchoBASE; EB3569; -. DR eggNOG; COG1172; Bacteria. DR HOGENOM; CLU_028880_0_0_6; -. DR InParanoid; P0AFS1; -. DR OMA; NTVVFQF; -. DR OrthoDB; 7947581at2; -. DR PhylomeDB; P0AFS1; -. DR BioCyc; EcoCyc:YDEZ-MONOMER; -. DR BioCyc; MetaCyc:YDEZ-MONOMER; -. DR PHI-base; PHI:9994; -. DR PRO; PR:P0AFS1; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P0AFS1; -. DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; NAS:ComplexPortal. DR GO; GO:0016020; C:membrane; NAS:ComplexPortal. DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc. DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro. DR GO; GO:1905887; P:autoinducer AI-2 transmembrane transport; IDA:EcoCyc. DR GO; GO:0009372; P:quorum sensing; NAS:ComplexPortal. DR CDD; cd06579; TM_PBP1_transp_AraH_like; 1. DR InterPro; IPR001851; ABC_transp_permease. DR NCBIfam; NF011612; PRK15038.1; 1. DR PANTHER; PTHR32196; ABC TRANSPORTER PERMEASE PROTEIN YPHD-RELATED-RELATED; 1. DR PANTHER; PTHR32196:SF71; AUTOINDUCER 2 IMPORT SYSTEM PERMEASE PROTEIN LSRD; 1. DR Pfam; PF02653; BPD_transp_2; 1. PE 1: Evidence at protein level; KW Cell inner membrane; Cell membrane; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..330 FT /note="Autoinducer 2 import system permease protein LsrD" FT /id="PRO_0000060248" FT TOPO_DOM 1..4 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 5..25 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 26..42 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 43..63 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 64..67 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 68..88 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 89..109 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 110..115 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 116..136 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 137..159 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 160..180 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 181..209 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 210..230 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 231..237 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 238..258 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 259..279 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 280..285 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 286..306 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 307..330 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" SQ SEQUENCE 330 AA; 34456 MW; 87CDB0958FB81C1E CRC64; MRIRYGWELA LAALLVIEIV AFGAINPRML DLNMLLFSTS DFICIGIVAL PLTMVIVSGG IDISFGSTIG LCAIALGVLF QSGVPMPLAI LLTLLLGALC GLINAGLIIY TKVNPLVITL GTLYLFAGSA LLLSGMAGAT GYEGIGGFPM AFTDFANLDV LGLPVPLIIF LICLLVFWLW LHKTHAGRNV FLIGQSPRVA LYSAIPVNRT LCALYAMTGL ASAVAAVLLV SYFGSARSDL GASFLMPAIT AVVLGGANIY GGSGSIIGTA IAVLLVGYLQ QGLQMAGVPN QVSSALSGAL LIVVVVGRSV SLHRQQIKEW LARRANNPLP //