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 03-JUL-2019, entry version 135. DE RecName: Full=Autoinducer 2 import ATP-binding protein LsrA; DE Short=AI-2 import ATP-binding protein LsrA; DE EC=3.6.3.-; 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., 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 [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., RA Mau B., 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 RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] 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 RT AI-2 in Escherichia coli."; RL J. Bacteriol. 187:238-248(2005). RN [6] 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 RT and uptake of extracellular autoinducer 2 in Escherichia coli."; RL J. Bacteriol. 187:2066-2076(2005). CC -!- FUNCTION: Part of the ABC transporter complex LsrABCD involved in CC autoinducer 2 (AI-2) import. Responsible for energy coupling to CC the transport system (Probable). This protein is essential for CC aerobic growth. {ECO:0000269|PubMed:15601708, ECO:0000305}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (LsrA), two transmembrane proteins (LsrC and LsrD) and a solute- CC binding protein (LsrB). {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; CC Peripheral membrane protein {ECO:0000305}. CC -!- INDUCTION: In the absence of AI-2, repressed by LsrR. Induced by CC AI-2, via release of the LsrR repressor. In the absence of CC glucose, induced by cAMP-CRP by direct binding to the upstream CC region of the lsr promoter. {ECO:0000269|PubMed:15601708, CC ECO:0000269|PubMed:15743955}. 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_LN832404.1. DR SMR; P77257; -. DR BioGrid; 4260226; 15. 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 EcoGene; EG13806; lsrA. DR eggNOG; ENOG4105C2J; Bacteria. DR eggNOG; COG1129; LUCA. DR InParanoid; P77257; -. DR KO; K10558; -. DR PhylomeDB; P77257; -. DR BioCyc; EcoCyc:YDEX-MONOMER; -. DR BioCyc; ECOL316407:JW1506-MONOMER; -. DR BioCyc; MetaCyc: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:0016887; F:ATPase activity; IEA:InterPro. 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 InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_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; Complete proteome; KW Hydrolase; Membrane; Nucleotide-binding; Reference proteome; Repeat; KW Transport. FT CHAIN 1 511 Autoinducer 2 import ATP-binding protein FT LsrA. FT /FTId=PRO_0000092321. FT DOMAIN 12 240 ABC transporter 1. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT DOMAIN 240 503 ABC transporter 2. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 44 51 ATP. {ECO:0000255|PROSITE- FT 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 //