ID LSRA_ECOLC Reviewed; 511 AA.
AC B1IRU7;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 86.
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=EcolC_2145;
OS Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS WDCM 00012 / Crooks).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=481805;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Ingram L., Richardson P.;
RT "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000946; ACA77785.1; -; Genomic_DNA.
DR RefSeq; WP_001194875.1; NZ_MTFT01000006.1.
DR AlphaFoldDB; B1IRU7; -.
DR SMR; B1IRU7; -.
DR KEGG; ecl:EcolC_2145; -.
DR HOGENOM; CLU_000604_92_3_6; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd03216; ABC_Carb_Monos_I; 1.
DR CDD; cd03215; ABC_Carb_Monos_II; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR43790:SF2; AUTOINDUCER 2 IMPORT ATP-BINDING PROTEIN LSRA; 1.
DR PANTHER; PTHR43790; CARBOHYDRATE TRANSPORT ATP-BINDING PROTEIN MG119-RELATED; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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_0000351290"
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; 55647 MW; B83BCCDBAEAC8B27 CRC64;
MQTSDTRALP LLCARSVYKQ YSGVNVLKGI DFTLHQGEVH ALLGGNGAGK STLMKIIAGI
TPADSGTLEI GGNNYARLTP VHAHQLGIYL VPQEPLLFPS LSIKENILFG LAKKQLSMQK
MKNLLAALGC QFDLHSLAGS LDVADRQMVE ILRGLMRDSR ILILDEPTAS LTPAETERLF
TRLQELLATG VGIVFISHKL PEIRQIADRI SVMRDGTIAL SGKTSELSTD DIIQAITPVV
REKSLSASQK LWLELPGNRP QHAAGTPVLT LENLTGEGFR NVSLTLNAGE ILGLAGLVGA
GRTELAETLY GLRTLRGGRI MLNGNEINKL STGERLLRGL VYLPEDRQSS GLNLDASLAW
NVCALTHNLR GFWAKTAKDN ATLERYRRAL NIKFNQPEQA ARTLSGGNQQ KILIAKCLEA
SPQVLIVDEP TRGVDVSARN DIYQLLRSIA AQNVAVLLIS SDLEEIELMA DRVYVMHQGE
IAHSALTGRD INVETIMRVA FGDSQRQEAS C
//
