LSRR_ECOLI
ID LSRR_ECOLI Reviewed; 317 AA.
AC P76141; P77190;
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=Transcriptional regulator LsrR;
GN Name=lsrR; Synonyms=ydeW; OrderedLocusNames=b1512, JW1505;
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], AND SEQUENCE REVISION TO
RP 239-317.
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.
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 FUNCTION.
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 FUNCTION AS A GLOBAL REGULATOR.
RX PubMed=17557827; DOI=10.1128/jb.00014-07;
RA Li J., Attila C., Wang L., Wood T.K., Valdes J.J., Bentley W.E.;
RT "Quorum sensing in Escherichia coli is signaled by AI-2/LsrR: effects on
RT small RNA and biofilm architecture.";
RL J. Bacteriol. 189:6011-6020(2007).
CC -!- FUNCTION: Regulates transcription of many different genes. In the
CC absence of autoinducer 2 (AI-2), represses transcription of the
CC lsrACDBFG operon and its own transcription. In the presence of AI-2,
CC LsrR is inactivated by binding phospho-AI-2, leading to the
CC transcription of the lsr genes. {ECO:0000269|PubMed:15601708,
CC ECO:0000269|PubMed:15743955, ECO:0000269|PubMed:17557827}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Autoregulated.
CC -!- SIMILARITY: Belongs to the SorC transcriptional regulatory family.
CC {ECO:0000305}.
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DR EMBL; U00096; AAC74585.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15192.2; -; Genomic_DNA.
DR PIR; C64905; C64905.
DR RefSeq; NP_416029.1; NC_000913.3.
DR RefSeq; WP_000154342.1; NZ_SSZK01000001.1.
DR PDB; 4GO1; X-ray; 3.00 A; A/B=1-317.
DR PDB; 4L4Y; X-ray; 1.90 A; A/B=53-317.
DR PDB; 4L4Z; X-ray; 2.30 A; A/B=53-317.
DR PDB; 4L50; X-ray; 2.10 A; A/B=53-317.
DR PDB; 4L51; X-ray; 1.90 A; A/B=53-317.
DR PDB; 4L5I; X-ray; 3.21 A; A/B/C/D=1-317.
DR PDB; 4L5J; X-ray; 2.60 A; A/B/C/D=1-317.
DR PDBsum; 4GO1; -.
DR PDBsum; 4L4Y; -.
DR PDBsum; 4L4Z; -.
DR PDBsum; 4L50; -.
DR PDBsum; 4L51; -.
DR PDBsum; 4L5I; -.
DR PDBsum; 4L5J; -.
DR AlphaFoldDB; P76141; -.
DR SMR; P76141; -.
DR BioGRID; 4260225; 8.
DR DIP; DIP-11688N; -.
DR IntAct; P76141; 5.
DR STRING; 511145.b1512; -.
DR jPOST; P76141; -.
DR PaxDb; P76141; -.
DR PRIDE; P76141; -.
DR EnsemblBacteria; AAC74585; AAC74585; b1512.
DR EnsemblBacteria; BAA15192; BAA15192; BAA15192.
DR GeneID; 946070; -.
DR KEGG; ecj:JW1505; -.
DR KEGG; eco:b1512; -.
DR PATRIC; fig|1411691.4.peg.755; -.
DR EchoBASE; EB3566; -.
DR eggNOG; COG2390; Bacteria.
DR HOGENOM; CLU_054506_0_1_6; -.
DR InParanoid; P76141; -.
DR OMA; CTVVQLT; -.
DR PhylomeDB; P76141; -.
DR BioCyc; EcoCyc:G6799-MON; -.
DR PRO; PR:P76141; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:2000142; P:regulation of DNA-templated transcription, initiation; IMP:EcoCyc.
DR GO; GO:0009408; P:response to heat; IMP:EcoCyc.
DR GO; GO:0006351; P:transcription, DNA-templated; IEP:EcoCyc.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR InterPro; IPR007324; Sugar-bd_dom_put.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF04198; Sugar-bind; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; DNA-binding; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..317
FT /note="Transcriptional regulator LsrR"
FT /id="PRO_0000062790"
FT DNA_BIND 33..52
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT CONFLICT 239..317
FT /note="GAVGDILGYFFDAKGDVVTNIKIHNELIGLPLSALKTIPVRVGVAGGENKAE
FT AIAAAMKGGYINALVTDQDTAAAILRS -> RGGWRHFRLLF (in Ref. 1)"
FT /evidence="ECO:0000305"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:4L5J"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:4L5J"
FT HELIX 44..57
FT /evidence="ECO:0007829|PDB:4L5J"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:4L5J"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:4L4Y"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:4L4Y"
FT HELIX 98..113
FT /evidence="ECO:0007829|PDB:4L4Y"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:4L4Y"
FT HELIX 126..141
FT /evidence="ECO:0007829|PDB:4L4Y"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:4L4Y"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:4L4Y"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:4L4Y"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:4GO1"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:4L5J"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:4L4Y"
FT HELIX 191..201
FT /evidence="ECO:0007829|PDB:4L4Y"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:4L4Y"
FT HELIX 213..218
FT /evidence="ECO:0007829|PDB:4L51"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:4L51"
FT HELIX 229..237
FT /evidence="ECO:0007829|PDB:4L4Y"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:4L4Y"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:4L4Y"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:4L4Y"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:4L4Y"
FT STRAND 276..282
FT /evidence="ECO:0007829|PDB:4L4Y"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:4L4Y"
FT HELIX 289..297
FT /evidence="ECO:0007829|PDB:4L4Y"
FT STRAND 302..307
FT /evidence="ECO:0007829|PDB:4L4Y"
FT HELIX 308..315
FT /evidence="ECO:0007829|PDB:4L4Y"
SQ SEQUENCE 317 AA; 33797 MW; F9EAA1FE716A1F65 CRC64;
MTINDSAISE QGMCEEEQVA RIAWFYYHDG LTQSEISDRL GLTRLKVSRL LEKGHQSGII
RVQINSRFEG CLEYETQLRR QFSLQHVRVI PGLADADVGG RLGIGAAHML MSLLQPQQML
AIGFGEATMN TLQRLSGFIS SQQIRLVTLS GGVGSYMTGI GQLNAACSVN IIPAPLRASS
ADIARTLKNE NCVKDVLLAA QAADVAIVGI GAVSQQDDAT IIRSGYISQG EQLMIGRKGA
VGDILGYFFD AKGDVVTNIK IHNELIGLPL SALKTIPVRV GVAGGENKAE AIAAAMKGGY
INALVTDQDT AAAILRS
