ID   LSRA_YERPA              Reviewed;         527 AA.
AC   Q1C138;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=YPA_3873;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(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; CP000308; ABG15834.1; -; Genomic_DNA.
DR   PIR; AC0051; AC0051.
DR   RefSeq; WP_002209192.1; NZ_CP009906.1.
DR   AlphaFoldDB; Q1C138; -.
DR   SMR; Q1C138; -.
DR   EnsemblBacteria; ABG15834; ABG15834; YPA_3873.
DR   GeneID; 57974198; -.
DR   KEGG; ypa:YPA_3873; -.
DR   OMA; ITHRFPE; -.
DR   Proteomes; UP000001971; 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..527
FT                   /note="Autoinducer 2 import ATP-binding protein LsrA"
FT                   /id="PRO_0000351311"
FT   DOMAIN          12..240
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          266..506
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          507..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..527
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         44..51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   527 AA;  56928 MW;  090646D82E1EB6B0 CRC64;
     MPHTVATPPP LLQVRGISKQ FSGVVVLKSI DFTLQPGQVH ALLGGNGAGK STLMKIIAGI
     LPPDTGVIEM NGQPCFNLTP AKAHQLGIYL VPQEPMLFAN LSVQENILFR LPKHQADKKK
     MAQLLKNLGC HLDLSVSAGS LEVADQQLVE IMRGLIRDSH ILILDEPTAS LTPAETHRLF
     SQIRMLLQQG VGVVFISHKL PEIRQLADWV SVMRDGGIAL SGATADFSTE DMIQAMTPEA
     QKGALTDSQK LWLELPGNRR AQSHAQSQQP VIHVHDLSGE GFAHISFHVQ AGEILGLAGV
     VGAGRTELAE TLYGLRPAST GNVILEEVNI TAMKTANRLA AGLVYLPEDR QASGLYLDAP
     LSWNVCALAH DRQGLWTQPA QEAAVLERYR RALNIKFSHL EQPVRTLSGG NQQKLLIAKC
     LEANPLLLII DEPTRGVDVS ARSDIYQLIR SIAEQQVAII FISSDLEEVV QMADRVLVMH
     QGEINGALSG AAMNVDTIMH MAFGEHRSAS EPQGGTASSA ENKGASC