ID LSRA_ECOLI Reviewed; 511 AA. AC P77257; P76879; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 23-FEB-2022, entry version 148. DE RecName: Full=Autoinducer 2 import ATP-binding protein LsrA; DE Short=AI-2 import ATP-binding protein LsrA; DE EC=7.6.2.13 {ECO:0000305|PubMed:15601708}; DE AltName: Full=EGO10A; GN Name=lsrA; Synonyms=ego, ydeX; OrderedLocusNames=b1513, JW1506; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Kwon H.B., Lee S.H., Choe M.H.; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. RN [2] 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 [3] 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 [4] 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 [5] RP DISRUPTION PHENOTYPE. RC STRAIN=CC118; RX PubMed=15380559; DOI=10.1016/j.resmic.2004.05.006; RA Serina S., Nozza F., Nicastro G., Faggioni F., Mottl H., Deho G., RA Polissi A.; RT "Scanning the Escherichia coli chromosome by random transposon mutagenesis RT and multiple phenotypic screening."; RL Res. Microbiol. 155:692-701(2004). RN [6] 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 [7] 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 [8] RP DISRUPTION PHENOTYPE. RC STRAIN=K12 / BW25113; RX PubMed=16738554; DOI=10.1038/msb4100050; RA Baba T., Ara T., Hasegawa M., Takai Y., Okumura Y., Baba M., Datsenko K.A., RA Tomita M., Wanner B.L., Mori H.; RT "Construction of Escherichia coli K-12 in-frame, single-gene knockout RT mutants: the Keio collection."; RL Mol. Syst. Biol. 2:2006.0008-2006.0008(2006). RN [9] RP DISRUPTION PHENOTYPE. RC STRAIN=K12 / BW25113; RX PubMed=29463657; DOI=10.1128/mbio.02096-17; RA Goodall E.C.A., Robinson A., Johnston I.G., Jabbari S., Turner K.A., RA Cunningham A.F., Lund P.A., Cole J.A., Henderson I.R.; RT "The essential genome of Escherichia coli K-12."; RL MBio 9:0-0(2018). CC -!- FUNCTION: Part of the ABC transporter complex LsrABCD involved in CC autoinducer 2 (AI-2) import. Responsible for energy coupling to the CC transport system. {ECO:0000305|PubMed:15601708}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H(2)O + (2R,4S)-2-methyl-2,3,3,4- CC tetrahydroxytetrahydrofuran-[AI-2-binding protein](Side 1) = ADP + CC phosphate + (2R,4S)-2-methyl-2,3,3,4-tetrahydroxytetrahydrofuran(Side CC 2) + [AI-2-binding protein](Side 1).; EC=7.6.2.13; CC Evidence={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|PubMed:15601708}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral CC membrane protein {ECO:0000305}. 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 -!- DISRUPTION PHENOTYPE: Serina et al. reported that the transposon CC insertion mutant is unable to grow in rich medium at optimal CC temperature (37 degrees Celsius), whereas it can grow in minimal medium CC at 37 degrees Celsius and in LD broth at 15 degrees Celsius CC (PubMed:15380559). In contrast, other studies showed that the gene is CC not essential for growth in Luria broth (LB) medium at 37 degrees CC Celsius (PubMed:16738554, PubMed:29463657). CC {ECO:0000269|PubMed:15380559, ECO:0000269|PubMed:16738554, CC ECO:0000269|PubMed:29463657}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. AI-2 CC autoinducer porter (TC 3.A.1.2.8) family. {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; AF089855; AAC61747.1; -; Genomic_DNA. DR EMBL; U00096; AAC74586.1; -; Genomic_DNA. DR EMBL; AP009048; BAA15200.1; -; Genomic_DNA. DR PIR; D64905; D64905. DR RefSeq; NP_416030.1; NC_000913.3. DR RefSeq; WP_001194860.1; NZ_SSZK01000001.1. DR SMR; P77257; -. DR BioGRID; 4260226; 15. DR BioGRID; 850052; 1. DR ComplexPortal; CPX-4315; Autoinducer-2 ABC transporter complex. DR IntAct; P77257; 3. DR STRING; 511145.b1513; -. DR TCDB; 3.A.1.2.8; the atp-binding cassette (abc) superfamily. DR jPOST; P77257; -. DR PaxDb; P77257; -. DR PRIDE; P77257; -. DR EnsemblBacteria; AAC74586; AAC74586; b1513. DR EnsemblBacteria; BAA15200; BAA15200; BAA15200. DR GeneID; 945680; -. DR KEGG; ecj:JW1506; -. DR KEGG; eco:b1513; -. DR PATRIC; fig|1411691.4.peg.754; -. DR EchoBASE; EB3567; -. DR eggNOG; COG1129; Bacteria. DR HOGENOM; CLU_000604_92_3_6; -. DR InParanoid; P77257; -. DR PhylomeDB; P77257; -. DR BioCyc; EcoCyc:YDEX-MONOMER; -. DR PRO; PR:P77257; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IEA:InterPro. DR GO; GO:1905887; P:autoinducer AI-2 transmembrane transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like_ATP-bd. DR InterPro; IPR017871; ABC_transporter-like_CS. DR InterPro; IPR030281; LsrA. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR43790:SF2; PTHR43790:SF2; 1. DR Pfam; PF00005; ABC_tran; 2. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. PE 1: Evidence at protein level; KW ATP-binding; Cell inner membrane; Cell membrane; Membrane; KW Nucleotide-binding; Reference proteome; Repeat; Translocase; Transport. FT CHAIN 1..511 FT /note="Autoinducer 2 import ATP-binding protein LsrA" FT /id="PRO_0000092321" FT DOMAIN 12..240 FT /note="ABC transporter 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT DOMAIN 240..503 FT /note="ABC transporter 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT NP_BIND 44..51 FT /note="ATP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" SQ SEQUENCE 511 AA; 55821 MW; CC399008BFFD55FA CRC64; MQTSDTRALP LLCARSVYKQ YSGVNVLKGI DFTLHQGEVH ALLGGNGAGK STLMKIIAGI TPADSGTLEI EGNNYVRLTP VHAHQLGIYL VPQEPLLFPS LSIKENILFG LAKKQLSMQK MKNLLAALGC QFDLHSLAGS LDVADRQMVE ILRGLMRDSR ILILDEPTAS LTPAETERLF SRLQELLATG VGIVFISHKL PEIRQIADRI SVMRDGTIAL SGKTSELSTD DIIQAITPAV REKSLSASQK LWLELPGNRP QHAAGTPVLT LENLTGEGFR NVSLTLNAGE ILGLAGLVGA GRTELAETLY GLRTLRGGRI MLNGKEINKL STGERLLRGL VYLPEDRQSS GLNLDASLAW NVCALTHNLR GFWAKTAKDN ATLERYRRAL NIKFNQPEQA ARTLSGGNQQ KILIAKCLEA SPQVLIVDEP TRGVDVSARN DIYQLLRSIA AQNVAVLLIS SDLEEIELMA DRVYVMHQGE ITHSALTERD INVETIMRVA FGDSQRQEAS C //