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Reviewed, UniProtKB/Swiss-Prot Q5HTR6 (LUXS_CAMJR)

Last modified January 19, 2010. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    S-ribosylhomocysteine lyase
    EC=4.4.1.21
Alternative name(s):
    Autoinducer-2 production protein luxS
    AI-2 synthesis protein
Gene names
Name: luxS
Ordered Locus Names: CJE1332
OrganismCampylobacter jejuni (strain RM1221) [Complete proteome] [HAMAP]
Taxonomic identifier195099 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length164 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD) By similarity. HAMAP MF_00091

Catalytic activity

S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione. HAMAP MF_00091

Cofactor

Binds 1 iron ion per subunit By similarity. HAMAP MF_00091

Subunit structure

Homodimer By similarity. HAMAP MF_00091

Sequence similarities

Belongs to the luxS family.

Ontologies

Keywords
   Biological processAutoinducer synthesis
Quorum sensing
   LigandIron
Metal-binding
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processquorum sensing

Inferred from electronic annotation. Source: HAMAP

   Molecular functionS-ribosylhomocysteine lyase activity

Inferred from electronic annotation. Source: HAMAP

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 164164S-ribosylhomocysteine lyase HAMAP MF_00091
PRO_0000172215

Sites

Metal binding541Iron By similarity
Metal binding581Iron By similarity
Metal binding1281Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HTR6-1 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 63FE7BDD1A9A1AC1

FASTA16418,271
        10         20         30         40         50         60 
MPLLDSFKVD HTKMPAPAVR LAKVMKTPKG DDISVFDLRF CIPNKDIMSE KGTHTLEHLF 

        70         80         90        100        110        120 
AGFMRDHLNS NSVEIIDISP MGCRTGFYMS LIGTPDEKSV AKAWEEAMKD VLSVSDQSKI 

       130        140        150        160 
PELNIYQCGT CAMHSLDEAK QIAQKVLNLG ISIMNNKELK LENA 

« Hide

References

[1]"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species."
Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., Ayodeji M.A., Shvartsbeyn A., Schatz M.C. expand/collapse author list , Badger J.H., Fraser C.M., Nelson K.E.
PLoS Biol. 3:72-85(2005) [PubMed: 15660156] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000025 Genomic DNA. Translation: AAW35653.1.
RefSeqYP_179319.1.

3D structure databases

SMRQ5HTR6. Positions 3-163.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5HTR6.

Genome annotation databases

GeneID3231839.
GenomeReviewsGene locus CJE1332 in contig CP000025_GR.
KEGGcjr:CJE1332.
NMPDRfig|195099.3.peg.1371.
TIGRCJE1332.

Phylogenomic databases

eggNOGCOG1854.
HOGENOMHBG347473.
OMAVRIAKTM.

Enzyme and pathway databases

BioCycCJEJ195099:CJE_1332-MONOMER.

Family and domain databases

HAMAPMF_00091. LuxS.
[Tree]
InterProIPR011249. Metalloenz_metal-bd.
IPR003815. S-ribosylhomocysteinase.
[Graphical view]
Gene3DG3DSA:3.30.1360.80. S-ribosylhomocysteinase. 1 hit.
PfamPF02664. LuxS. 1 hit.
[Graphical view]
PIRSFPIRSF006160. AI2. 1 hit.
PRINTSPR01487. LUXSPROTEIN.
ProDomPD013172. S-ribosylhomocysteinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Entry information

Entry nameLUXS_CAMJR
AccessionPrimary (citable) accession number: Q5HTR6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: February 15, 2005
Last modified: January 19, 2010
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents