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P64461 (LSRG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Autoinducer 2-degrading protein lsrG

Short name=AI-2-degrading protein lsrG
Gene names
Name:lsrG
Synonyms:yneC
Ordered Locus Names:b1518, JW1511
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length96 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the degradation of phospho-AI-2, thereby terminating induction of the lsr operon and closing the AI-2 signaling cycle. Catalyzes the cleavage of phosphorylated 4,5-dihydroxy-2,3-pentanedione (P-DPD) to 2-phosphoglycolic acid (PG) and another three-carbon compound. Ref.5

Subcellular location

Cytoplasm Potential.

Induction

In the absence of AI-2, repressed by lsrR. Induced by AI-2, via release of the lsrR repressor. In the absence of glucose, induced by cAMP-CRP by direct binding to the upstream region of the lsr promoter. Ref.3 Ref.4

Sequence similarities

Belongs to the lsrG family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncatalytic activity

Inferred from direct assay Ref.5. Source: EcoCyc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

nadEP188431EBI-1124339,EBI-548960

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 9696Autoinducer 2-degrading protein lsrG
PRO_0000168947

Sequences

Sequence LengthMass (Da)Tools
P64461 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 138099193F125EB8

FASTA9611,255
        10         20         30         40         50         60 
MHVTLVEINV HEDKVDEFIE VFRQNHLGSV QEEGNLRFDV LQDPEVNSRF YIYEAYKDED 

        70         80         90 
AVAFHKTTPH YKTCVAKLES LMTGPRKKRL FNGLMP 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[2]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"Regulation of uptake and processing of the quorum-sensing autoinducer AI-2 in Escherichia coli."
Xavier K.B., Bassler B.L.
J. Bacteriol. 187:238-248(2005) [PubMed: 15601708] [Abstract]
Cited for: INDUCTION.
Strain: K12 / MG1655 / ATCC 47076.
[4]"Cyclic AMP (cAMP) and cAMP receptor protein influence both synthesis and uptake of extracellular autoinducer 2 in Escherichia coli."
Wang L., Hashimoto Y., Tsao C.-Y., Valdes J.J., Bentley W.E.
J. Bacteriol. 187:2066-2076(2005) [PubMed: 15743955] [Abstract]
Cited for: INDUCTION.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Phosphorylation and processing of the quorum-sensing molecule autoinducer-2 in enteric bacteria."
Xavier K.B., Miller S.T., Lu W., Kim J.H., Rabinowitz J., Pelczer I., Semmelhack M.F., Bassler B.L.
ACS Chem. Biol. 2:128-136(2007) [PubMed: 17274596] [Abstract]
Cited for: FUNCTION IN PHOSPHO-AI-2 DEGRADATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00096 Genomic DNA. Translation: AAC74591.1.
AP009048 Genomic DNA. Translation: BAE76458.1.
PIRA64906.
RefSeqNP_416035.1. NC_000913.2.

3D structure databases

ProteinModelPortalP64461.
SMRP64461. Positions 1-96.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-47853N.
IntActP64461. 3 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000002699; EBESCP00000002699; EBESCG00000002200.
EBESCT00000017115; EBESCP00000016406; EBESCG00000016174.
GeneID946073.
GenomeReviewsGene locus JW1511 in contig AP009048_GR.
Gene locus b1518 in contig U00096_GR.
KEGGecj:JW1511.
eco:b1518.
PATRIC32118332. VBIEscCol129921_1586.

Organism-specific databases

EchoBASEEB3572.
EcoGeneEG13811. lsrG.

Phylogenomic databases

eggNOGCOG1359.
GeneTreeEBGT00050000011886.
HOGENOMHBG693987.
OMAKKTPHYL.
PhylomeDBP64461.
ProtClustDBPRK10486.

Enzyme and pathway databases

BioCycEcoCyc:G6805-MONOMER.
MetaCyc:G6805-MONOMER.

Gene expression databases

GenevestigatorP64461.

Family and domain databases

InterProIPR007138. Antibiotic_mOase.
IPR011008. Dimeric_a/b-barrel.
[Graphical view]
KOK11530.
PfamPF03992. ABM. 1 hit.
[Graphical view]
SUPFAMSSF54909. Dimer_A_B_barrel. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLSRG_ECOLI
AccessionPrimary (citable) accession number: P64461
Secondary accession number(s): P76144, Q2MB98
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: January 25, 2012
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families