LSRA_YERPG
ID LSRA_YERPG Reviewed; 527 AA.
AC A9R074;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=YpAngola_A0858;
OS Yersinia pestis bv. Antiqua (strain Angola).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Angola;
RX PubMed=20061468; DOI=10.1128/jb.01518-09;
RA Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA Achtman M., Lindler L.E., Ravel J.;
RT "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT new insights into the evolution and pangenome of the plague bacterium.";
RL J. Bacteriol. 192:1685-1699(2010).
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; CP000901; ABX87181.1; -; Genomic_DNA.
DR RefSeq; WP_002209192.1; NZ_CP009935.1.
DR AlphaFoldDB; A9R074; -.
DR SMR; A9R074; -.
DR GeneID; 57974198; -.
DR KEGG; ypg:YpAngola_A0858; -.
DR PATRIC; fig|349746.12.peg.1809; -.
DR OMA; ITHRFPE; -.
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_0000351310"
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