ID   LSRA_PHOTE              Reviewed;         520 AA.
AC   Q2PBM3;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 60.
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;
OS   Photorhabdus temperata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=574560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C1 / NC19;
RX   PubMed=16385072; DOI=10.1128/jb.188.2.809-814.2006;
RA   Gaudriault S., Duchaud E., Lanois A., Canoy A.-S., Bourot S., DeRose R.,
RA   Kunst F., Boemare N., Givaudan A.;
RT   "Whole-genome comparison between Photorhabdus strains to identify genomic
RT   regions involved in the specificity of nematode interaction.";
RL   J. Bacteriol. 188:809-814(2006).
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; AJ967009; CAI91185.1; -; Genomic_DNA.
DR   RefSeq; WP_036843258.1; NZ_MBJU01000082.1.
DR   AlphaFoldDB; Q2PBM3; -.
DR   SMR; Q2PBM3; -.
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..520
FT                   /note="Autoinducer 2 import ATP-binding protein LsrA"
FT                   /id="PRO_0000351299"
FT   DOMAIN          12..240
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          264..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   520 AA;  57213 MW;  A04ED2E6FF62F126 CRC64;
     MLHNNTAVPP LLEVSGISKQ FSGVMVLKHI DFTLLPGQIH ALLGGNGAGK STLMKIIAGI
     EQPDKGSIKI DGNNVSHLNP TKAHQLGIYL IPQEPLLFPN LSVQENILFR LPKHQADKAR
     MKHLLELLGC QLDLNANAGS LNVADQQLVE VMRGLIRNSN VLILDEPTAS LTPAETERLF
     TQLRELQQQS VGIIFISHKI PEIHQLADQV SVMRDGGIAL SGKTCDYTTD DIIRAITPAA
     KNKPLTDTEK RWSELNDNPQ KTSSDLPVLT VTDLNGEGFR NITLSVKPGE ILGLAGVVGA
     GRTELAETLY GLRPVLSGEI KLKQCPITRL KTVQRLKQGL VYLPEDRQSS GLFPDSSLSW
     NICSLTHNNR TFWVHPTYDA TVVERYRQAL NIKFSHINQP VKTLSGGNQQ KILIAKCLEA
     HPAVLIIDEP TRGVDIAARN DIYQLIHNIA QQQVAIIFIS SDLDEVVQMA DRVLVMHQGE
     INGELTKQQI DVDTIMHIAF GEHKSQQAVS TIKTDKAASC