ID   LSRA_ECOHS              Reviewed;         511 AA.
AC   A8A066;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Autoinducer 2 import ATP-binding protein LsrA {ECO:0000250|UniProtKB:P77257};
DE            Short=AI-2 import ATP-binding protein LsrA {ECO:0000250|UniProtKB:P77257};
DE            EC=7.6.2.13 {ECO:0000250|UniProtKB:P77257};
GN   Name=lsrA; OrderedLocusNames=EcHS_A1595;
OS   Escherichia coli O9:H4 (strain HS).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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:0000250|UniProtKB:P77257}.
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:0000250|UniProtKB:P77257};
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:0000250|UniProtKB:P77257}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P77257}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P77257}.
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; CP000802; ABV05920.1; -; Genomic_DNA.
DR   RefSeq; WP_001194891.1; NC_009800.1.
DR   AlphaFoldDB; A8A066; -.
DR   SMR; A8A066; -.
DR   KEGG; ecx:EcHS_A1595; -.
DR   HOGENOM; CLU_000604_92_3_6; -.
DR   OMA; ITHRFPE; -.
DR   Proteomes; UP000001123; 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   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Repeat; Translocase; Transport.
FT   CHAIN           1..511
FT                   /note="Autoinducer 2 import ATP-binding protein LsrA"
FT                   /id="PRO_0000351295"
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;  55637 MW;  6B628F079C52A4B1 CRC64;
     MQTSDTRALP LLCARSVYKQ YSGVNVLKGI DFTLHQGEVH ALLGGNGAGK STLMKIIAGI
     TPADSGTLEI GGNNYARLTP VHAHQLGIYL VPQEPLLFSS LSIKENILFG LAKKQLSMQK
     MKNLLAALGC QFDLHSLAGS LDVADRQMVE ILRGLMRDSR ILILDEPTAS LTPAETERLF
     TRLQELLATG VGIVFISHKL PEIRQIADRI SVMRDGTIAL SGKTSELSTD DIIQAITPVV
     REKSLSASQK LWLELPGNRP QHAAGTPVLT LENLTGEGFR NVSLTLNAGE ILGLAGLVGA
     GRTELAETLY GLRTLRGGRI MLNGNEINKL STGERLLRGL VYLPEDRQSS GLNLDASLAW
     NVCALTHNLR GFWAKTAKDN ATLERYRRAL NIKFNQPEQA ARTLSGGNQQ KILIAKCLEA
     SPQVLIVDEP TRGVDVSARN DIYQLLRSIA AQNVAVLLIS SDLEEIELMA DRVYVMHQGE
     IAHSALTGRD INVETIMRVA FGDSQRQEAS C