LSRC_ECOLI
ID LSRC_ECOLI Reviewed; 342 AA.
AC P77672;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Autoinducer 2 import system permease protein LsrC;
DE Short=AI-2 import system permease protein LsrC;
GN Name=lsrC; Synonyms=ydeY; OrderedLocusNames=b1514, JW1507;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION IN AI-2 IMPORT, AND INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15601708; DOI=10.1128/jb.187.1.238-248.2005;
RA Xavier K.B., Bassler B.L.;
RT "Regulation of uptake and processing of the quorum-sensing autoinducer AI-2
RT in Escherichia coli.";
RL J. Bacteriol. 187:238-248(2005).
RN [5]
RP INDUCTION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=15743955; DOI=10.1128/jb.187.6.2066-2076.2005;
RA Wang L., Hashimoto Y., Tsao C.-Y., Valdes J.J., Bentley W.E.;
RT "Cyclic AMP (cAMP) and cAMP receptor protein influence both synthesis and
RT uptake of extracellular autoinducer 2 in Escherichia coli.";
RL J. Bacteriol. 187:2066-2076(2005).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Part of the ABC transporter complex LsrABCD involved in
CC autoinducer 2 (AI-2) import. Probably responsible for the translocation
CC of the substrate across the membrane (Probable).
CC {ECO:0000305|PubMed:15601708}.
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:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- INDUCTION: In the absence of AI-2, repressed by LsrR. Induced by AI-2,
CC via release of the LsrR repressor. In the absence of glucose, induced
CC by cAMP-CRP by direct binding to the upstream region of the lsr
CC promoter. {ECO:0000269|PubMed:15601708, ECO:0000269|PubMed:15743955}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. AraH/RbsC subfamily. {ECO:0000305}.
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DR EMBL; U00096; AAC74587.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15201.1; -; Genomic_DNA.
DR PIR; E64905; E64905.
DR RefSeq; NP_416031.1; NC_000913.3.
DR RefSeq; WP_000911184.1; NZ_LN832404.1.
DR AlphaFoldDB; P77672; -.
DR BioGRID; 4260227; 12.
DR ComplexPortal; CPX-4315; Autoinducer-2 ABC transporter complex.
DR DIP; DIP-11689N; -.
DR STRING; 511145.b1514; -.
DR TCDB; 3.A.1.2.8; the atp-binding cassette (abc) superfamily.
DR jPOST; P77672; -.
DR PaxDb; P77672; -.
DR PRIDE; P77672; -.
DR EnsemblBacteria; AAC74587; AAC74587; b1514.
DR EnsemblBacteria; BAA15201; BAA15201; BAA15201.
DR GeneID; 946105; -.
DR KEGG; ecj:JW1507; -.
DR KEGG; eco:b1514; -.
DR PATRIC; fig|1411691.4.peg.753; -.
DR EchoBASE; EB3568; -.
DR eggNOG; COG1172; Bacteria.
DR HOGENOM; CLU_028880_0_1_6; -.
DR InParanoid; P77672; -.
DR OMA; KRMLKMH; -.
DR PhylomeDB; P77672; -.
DR BioCyc; EcoCyc:YDEY-MON; -.
DR BioCyc; MetaCyc:YDEY-MON; -.
DR PRO; PR:P77672; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:1905887; P:autoinducer AI-2 transmembrane transport; IC:ComplexPortal.
DR GO; GO:0009372; P:quorum sensing; IC:ComplexPortal.
DR InterPro; IPR001851; ABC_transp_permease.
DR Pfam; PF02653; BPD_transp_2; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..342
FT /note="Autoinducer 2 import system permease protein LsrC"
FT /id="PRO_0000060247"
FT TOPO_DOM 1..13
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..69
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..212
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..283
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..342
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 342 AA; 36395 MW; 419E505026ABDE33 CRC64;
MLKFIQNNRE ITALLAVVLL FVLPGFLDRQ YLSVQTLTMV YSSAQILILL AMGATLVMLT
RNIDVSVGSI TGMCAVLLGM LLNAGYSLPV ACVATLLLGL LAGFFNGVLV AWLKIPAIVA
TLGTLGLYRG IMLLWTGGKW IEGLPAELKQ LSAPLLLGVS AIGWLTIILV AFMAWLLAKT
AFGRSFYATG DNLQGARQLG VRTEAIRIVA FSLNGCMAAL AGIVFASQIG FIPNQTGTGL
EMKAIAACVL GGISLLGGSG AIIGAVLGAW FLTQIDSVLV LLRIPAWWND FIAGLVLLAV
LVFDGRLRCA LERNLRRQKY ARFMTPPPSV KPASSGKKRE AA
