LSRG_ECOLI
ID LSRG_ECOLI Reviewed; 96 AA.
AC P64461; P76144; Q2MB98;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=(4S)-4-hydroxy-5-phosphonooxypentane-2,3-dione isomerase {ECO:0000255|HAMAP-Rule:MF_02051};
DE EC=5.3.1.32 {ECO:0000255|HAMAP-Rule:MF_02051, ECO:0000269|PubMed:21454635};
DE AltName: Full=Autoinducer 2-degrading protein LsrG {ECO:0000255|HAMAP-Rule:MF_02051};
DE Short=AI-2-degrading protein LsrG {ECO:0000255|HAMAP-Rule:MF_02051};
DE AltName: Full=Phospho-(S)-4,5-dihydroxy-2,3-pentanedione isomerase {ECO:0000255|HAMAP-Rule:MF_02051, ECO:0000303|PubMed:21454635};
DE AltName: Full=Phospho-AI-2 isomerase {ECO:0000255|HAMAP-Rule:MF_02051};
GN Name=lsrG {ECO:0000255|HAMAP-Rule:MF_02051}; Synonyms=yneC;
GN OrderedLocusNames=b1518, JW1511;
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 / 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 [2]
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 [3]
RP 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 [4]
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 [5]
RP FUNCTION IN PHOSPHO-AI-2 DEGRADATION.
RX PubMed=17274596; DOI=10.1021/cb600444h;
RA Xavier K.B., Miller S.T., Lu W., Kim J.H., Rabinowitz J., Pelczer I.,
RA Semmelhack M.F., Bassler B.L.;
RT "Phosphorylation and processing of the quorum-sensing molecule autoinducer-
RT 2 in enteric bacteria.";
RL ACS Chem. Biol. 2:128-136(2007).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP SUBUNIT, AND MUTAGENESIS OF ASN-25; GLU-54; HIS-65 AND HIS-70.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21454635; DOI=10.1074/jbc.m111.230227;
RA Marques J.C., Lamosa P., Russell C., Ventura R., Maycock C.,
RA Semmelhack M.F., Miller S.T., Xavier K.B.;
RT "Processing the interspecies quorum-sensing signal autoinducer-2 (AI-2):
RT characterization of phospho-(S)-4,5-dihydroxy-2,3-pentanedione
RT isomerization by LsrG protein.";
RL J. Biol. Chem. 286:18331-18343(2011).
CC -!- FUNCTION: Involved in the degradation of phospho-AI-2, thereby
CC terminating induction of the lsr operon and closing the AI-2 signaling
CC cycle. Catalyzes the conversion of (4S)-4-hydroxy-5-
CC phosphonooxypentane-2,3-dione (P-DPD) to 3-hydroxy-5-
CC phosphonooxypentane-2,4-dione (P-HPD). {ECO:0000255|HAMAP-
CC Rule:MF_02051, ECO:0000269|PubMed:17274596,
CC ECO:0000269|PubMed:21454635}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-hydroxy-3,4-dioxopentyl phosphate = 3-hydroxy-2,4-
CC dioxopentyl phosphate; Xref=Rhea:RHEA:44360, ChEBI:CHEBI:71677,
CC ChEBI:CHEBI:84359; EC=5.3.1.32; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02051, ECO:0000269|PubMed:21454635};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02051,
CC ECO:0000269|PubMed:21454635}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02051}.
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 LsrG family. {ECO:0000255|HAMAP-
CC Rule:MF_02051}.
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DR EMBL; U00096; AAC74591.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76458.1; -; Genomic_DNA.
DR PIR; A64906; A64906.
DR RefSeq; NP_416035.1; NC_000913.3.
DR RefSeq; WP_000558527.1; NZ_STEB01000003.1.
DR PDB; 3QMQ; X-ray; 1.80 A; A/B/C/D=1-96.
DR PDBsum; 3QMQ; -.
DR AlphaFoldDB; P64461; -.
DR SMR; P64461; -.
DR BioGRID; 4260228; 12.
DR BioGRID; 850433; 1.
DR DIP; DIP-47853N; -.
DR IntAct; P64461; 6.
DR STRING; 511145.b1518; -.
DR jPOST; P64461; -.
DR PaxDb; P64461; -.
DR PRIDE; P64461; -.
DR EnsemblBacteria; AAC74591; AAC74591; b1518.
DR EnsemblBacteria; BAE76458; BAE76458; BAE76458.
DR GeneID; 58461895; -.
DR GeneID; 946073; -.
DR KEGG; ecj:JW1511; -.
DR KEGG; eco:b1518; -.
DR PATRIC; fig|1411691.4.peg.749; -.
DR EchoBASE; EB3572; -.
DR eggNOG; COG1359; Bacteria.
DR HOGENOM; CLU_131496_3_0_6; -.
DR InParanoid; P64461; -.
DR OMA; DTVAPMM; -.
DR PhylomeDB; P64461; -.
DR BioCyc; EcoCyc:G6805-MON; -.
DR BioCyc; MetaCyc:G6805-MON; -.
DR PRO; PR:P64461; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0002952; F:(4S)-4-hydroxy-5-phosphonooxypentane-2,3-dione isomerase activity; IDA:EcoCyc.
DR GO; GO:0003824; F:catalytic activity; IBA:GO_Central.
DR GO; GO:0016861; F:intramolecular oxidoreductase activity, interconverting aldoses and ketoses; IEA:UniProtKB-UniRule.
DR GO; GO:0016853; F:isomerase activity; IDA:EcoCyc.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR HAMAP; MF_02051; LsrG; 1.
DR InterPro; IPR007138; ABM_dom.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR033672; LsrG.
DR Pfam; PF03992; ABM; 1.
DR SUPFAM; SSF54909; SSF54909; 1.
DR PROSITE; PS51725; ABM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isomerase; Reference proteome.
FT CHAIN 1..96
FT /note="(4S)-4-hydroxy-5-phosphonooxypentane-2,3-dione
FT isomerase"
FT /id="PRO_0000168947"
FT DOMAIN 2..91
FT /note="ABM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02051"
FT MUTAGEN 25
FT /note="N->A: 3-fold lower specific activity."
FT /evidence="ECO:0000269|PubMed:21454635"
FT MUTAGEN 54
FT /note="E->A: No activity."
FT /evidence="ECO:0000269|PubMed:21454635"
FT MUTAGEN 65
FT /note="H->A: No activity."
FT /evidence="ECO:0000269|PubMed:21454635"
FT MUTAGEN 70
FT /note="H->A: 100-fold lower specific activity."
FT /evidence="ECO:0000269|PubMed:21454635"
SQ SEQUENCE 96 AA; 11255 MW; 138099193F125EB8 CRC64;
MHVTLVEINV HEDKVDEFIE VFRQNHLGSV QEEGNLRFDV LQDPEVNSRF YIYEAYKDED
AVAFHKTTPH YKTCVAKLES LMTGPRKKRL FNGLMP
