LSRD_ECOLI
ID LSRD_ECOLI Reviewed; 330 AA.
AC P0AFS1; P76881; P77651;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Autoinducer 2 import system permease protein LsrD;
DE Short=AI-2 import system permease protein LsrD;
GN Name=lsrD; Synonyms=ydeZ; OrderedLocusNames=b1515, JW1508;
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; AAC74588.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15202.1; -; Genomic_DNA.
DR PIR; F64905; F64905.
DR RefSeq; NP_416032.1; NC_000913.3.
DR RefSeq; WP_001222721.1; NZ_STEB01000003.1.
DR AlphaFoldDB; P0AFS1; -.
DR BioGRID; 4259116; 6.
DR ComplexPortal; CPX-4315; Autoinducer-2 ABC transporter complex.
DR STRING; 511145.b1515; -.
DR TCDB; 3.A.1.2.8; the atp-binding cassette (abc) superfamily.
DR PaxDb; P0AFS1; -.
DR PRIDE; P0AFS1; -.
DR EnsemblBacteria; AAC74588; AAC74588; b1515.
DR EnsemblBacteria; BAA15202; BAA15202; BAA15202.
DR GeneID; 66674631; -.
DR GeneID; 946264; -.
DR KEGG; ecj:JW1508; -.
DR KEGG; eco:b1515; -.
DR PATRIC; fig|1411691.4.peg.752; -.
DR EchoBASE; EB3569; -.
DR eggNOG; COG1172; Bacteria.
DR HOGENOM; CLU_028880_0_0_6; -.
DR InParanoid; P0AFS1; -.
DR OMA; LSLHREW; -.
DR PhylomeDB; P0AFS1; -.
DR BioCyc; EcoCyc:YDEZ-MON; -.
DR BioCyc; MetaCyc:YDEZ-MON; -.
DR PRO; PR:P0AFS1; -.
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..330
FT /note="Autoinducer 2 import system permease protein LsrD"
FT /id="PRO_0000060248"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..42
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..159
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..237
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..285
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..330
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 330 AA; 34456 MW; 87CDB0958FB81C1E CRC64;
MRIRYGWELA LAALLVIEIV AFGAINPRML DLNMLLFSTS DFICIGIVAL PLTMVIVSGG
IDISFGSTIG LCAIALGVLF QSGVPMPLAI LLTLLLGALC GLINAGLIIY TKVNPLVITL
GTLYLFAGSA LLLSGMAGAT GYEGIGGFPM AFTDFANLDV LGLPVPLIIF LICLLVFWLW
LHKTHAGRNV FLIGQSPRVA LYSAIPVNRT LCALYAMTGL ASAVAAVLLV SYFGSARSDL
GASFLMPAIT AVVLGGANIY GGSGSIIGTA IAVLLVGYLQ QGLQMAGVPN QVSSALSGAL
LIVVVVGRSV SLHRQQIKEW LARRANNPLP
