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-AUG-2022, entry version 150.
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 + H2O + (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-tetrahydroxytetrahydrofuranSide
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}.
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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   AlphaFoldDB; P77257; -.
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   OMA; ITHRFPE; -.
DR   PhylomeDB; P77257; -.
DR   BioCyc; EcoCyc:YDEX-MON; -.
DR   BioCyc; MetaCyc:YDEX-MON; -.
DR   PRO; PR:P77257; -.
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:0016020; C:membrane; IC:ComplexPortal.
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; IC:ComplexPortal.
DR   GO; GO:0009372; P:quorum sensing; IC:ComplexPortal.
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   BINDING         44..51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
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