ID   LSRA_SALCH              Reviewed;         511 AA.
AC   P0C886;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 43.
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=SCH_3963.1;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AE017220; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AE017220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P0C886; -.
DR   SMR; P0C886; -.
DR   Proteomes; UP000000538; 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_0000351300"
FT   DOMAIN          12..240
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          263..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;  55491 MW;  92CD4168DDFD80D9 CRC64;
     MQISHNTASP LICVQNIYKS YSGVEVLKGI DFTLHAGEVH ALLGGNGAGK STLMKIIAGI
     VPPDGGTIDI AGVRCSHLTP LKAHQYGIYL VPQEPLLFPS LSVRENILFG LQGRQASTEK
     MQQLLKAMGC QLDPASAAGT LDVADRQIVE IMRGLMRDSR ILILDEPTAS LTPAETDRLF
     TRLQELLKKG VGIVFISHKL PEIRQLAHCV SVMRDGKIAL FGKTHDLSTD EIIQAITPAT
     QGVSLSASQK LWLELPGSRP QNERGATVLA LESLTGEGFM NINLEVRAGE ILGLAGLVGA
     GRTELAETLY GIRPVNAGRM LFNGEEINAL TTQQRLQLGL VYLPEDRQSS GLYLDASLAW
     NVCSLTHNQK GFWIKPQRDN ATLERYHRAL NIKLNNAEQA ARTLSGGNQQ KVLIAKCLEA
     SPQLLIVDEP TRGVDVSARS DIYQLLRSIA QQNVAVLFIS SDLEEIEQMA DRVYVMHQGE
     LGGPALCGEE INVDTIMHVA FGEHGASEAT C