LSRA_ECO57
ID LSRA_ECO57 Reviewed; 511 AA.
AC Q8XAY7; Q7ADZ7;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 132.
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=Z2192, ECs2120;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG56253.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB35543.1; -; Genomic_DNA.
DR PIR; A85724; A85724.
DR PIR; H90893; H90893.
DR RefSeq; NP_310147.1; NC_002695.1.
DR RefSeq; WP_001194917.1; NZ_SEKU01000015.1.
DR AlphaFoldDB; Q8XAY7; -.
DR SMR; Q8XAY7; -.
DR STRING; 155864.EDL933_2125; -.
DR EnsemblBacteria; AAG56253; AAG56253; Z2192.
DR EnsemblBacteria; BAB35543; BAB35543; ECs_2120.
DR GeneID; 917319; -.
DR KEGG; ece:Z2192; -.
DR KEGG; ecs:ECs_2120; -.
DR PATRIC; fig|386585.9.peg.2226; -.
DR eggNOG; COG1129; Bacteria.
DR HOGENOM; CLU_000604_92_3_6; -.
DR OMA; ITHRFPE; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome; Repeat; Translocase; Transport.
FT CHAIN 1..511
FT /note="Autoinducer 2 import ATP-binding protein LsrA"
FT /id="PRO_0000351294"
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; 55686 MW; 02E570D6215E2F1E CRC64;
MQTSDTRALP LLCARSVYKQ YSGVNVLKGI DFTLHQGEVH ALLGGNGAGK STLMKIIAGI
TSADSGTLEI GGNNYARLTP VHAHQLGIYL VPQEPLLFPS LSIKENILFG LAKKQLSMQK
MKNLLAALGC QFDLHSLAGS LDVADRQMVE ILRGLMRDSR ILILDEPTAS LTPAETERLF
TRLQELLATG VGIVFISHKL PEIRQIADRI SVMRDGTIAL SGKTSELSTD DIIQAITPAV
REKSLSASQK LWLELPGNRP QHAAGTSVLT LENLTGEGFR NVSLTLNAGE ILGLAGLVGA
GRTELAETLY GLRTLRGGRI MLNDKEINRL STGERLLRGL VYLPEDRQSS GLNLDASLAW
NVCALTHNLR GFWAKTAKDN ATLELYRRAL NIKYNQPEQA ARTLSGGNQQ KILIAKCLEA
SPQVLIVDEP TRGVDVSARN DIYQLLRSIA AQNVAVLLIS SDLEEIELMA DRVYVMHQGE
ITHSALTGRD INVETIMRVA FGDSQRQEAA C
