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O34667 (LUXS_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
S-ribosylhomocysteine lyase

EC=4.4.1.21
Alternative name(s):
AI-2 synthesis protein
Autoinducer-2 production protein LuxS
Gene names
Name:luxS
Synonyms:ytjB
Ordered Locus Names:BSU30670
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length157 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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). HAMAP-Rule MF_00091

Catalytic activity

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

Cofactor

Binds 1 iron ion per subunit. Ref.3

Subunit structure

Homodimer.

Sequence similarities

Belongs to the LuxS family.

Ontologies

Keywords
   Biological processAutoinducer synthesis
Quorum sensing
   LigandIron
Metal-binding
   Molecular functionLyase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processquorum sensing

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionS-ribosylhomocysteine lyase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

iron ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 157157S-ribosylhomocysteine lyase HAMAP-Rule MF_00091
PRO_0000172211

Sites

Metal binding541Iron
Metal binding581Iron
Metal binding1261Iron

Experimental info

Mutagenesis571E → A or Q: Complete loss of activity. Ref.3
Mutagenesis571E → D: 220-fold decrease in activity. Ref.3
Mutagenesis841C → A: Complete loss of activity. Ref.3
Mutagenesis841C → D or S: Almost complete loss of activity. Ref.3

Secondary structure

........................... 157
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O34667 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: DD011A2A88BD2FFB

FASTA15717,714
        10         20         30         40         50         60 
MPSVESFELD HNAVVAPYVR HCGVHKVGTD GVVNKFDIRF CQPNKQAMKP DTIHTLEHLL 

        70         80         90        100        110        120 
AFTIRSHAEK YDHFDIIDIS PMGCQTGYYL VVSGEPTSAE IVDLLEDTMK EAVEITEIPA 

       130        140        150 
ANEKQCGQAK LHDLEGAKRL MRFWLSQDKE ELLKVFG 

« Hide

References

« Hide 'large scale' references
[1]"Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region."
Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.
Microbiology 143:3431-3441(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"S-ribosylhomocysteinase (LuxS) is a mononuclear iron protein."
Zhu J., Dizin E., Hu X., Wavreille A.-S., Park J., Pei D.
Biochemistry 42:4717-4726(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: COFACTOR, CHARACTERIZATION, MUTAGENESIS OF GLU-57 AND CYS-84.
[4]"The 1.2 A structure of a novel quorum-sensing protein, Bacillus subtilis LuxS."
Ruzheinikov S.N., Das S.K., Sedelnikova S.E., Hartley A., Foster S.J., Horsburgh M.J., Cox A.G., McCleod C.W., Mekhalfia A., Blackburn G.M., Rice D.W., Baker P.J.
J. Mol. Biol. 313:111-122(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS).
[5]"Crystal structure of the quorum-sensing protein LuxS reveals a catalytic metal site."
Hilgers M.T., Ludwig M.L.
Proc. Natl. Acad. Sci. U.S.A. 98:11169-11174(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF008220 Genomic DNA. Translation: AAC00235.1.
AL009126 Genomic DNA. Translation: CAB15045.1.
PIRA69994.
RefSeqNP_390945.1. NC_000964.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IE0X-ray1.60A1-157[»]
1J98X-ray1.20A1-157[»]
1JQWX-ray2.30A1-157[»]
1JVIX-ray2.20A1-157[»]
1YCLX-ray1.80A2-157[»]
2FQOX-ray1.87A1-157[»]
2FQTX-ray1.79A1-157[»]
ProteinModelPortalO34667.
SMRO34667. Positions 4-157.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU30670.

Chemistry

BindingDBO34667.
ChEMBLCHEMBL5171.

Proteomic databases

PaxDbO34667.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15045; CAB15045; BSU30670.
GeneID937106.
KEGGbsu:BSU30670.
PATRIC18978038. VBIBacSub10457_3207.

Organism-specific databases

GenoListBSU30670. [Micado]

Phylogenomic databases

eggNOGCOG1854.
HOGENOMHOG000040372.
KOK07173.
OMAEFRAVIW.
OrthoDBEOG68WRBM.
PhylomeDBO34667.

Enzyme and pathway databases

BioCycBSUB:BSU30670-MONOMER.
MetaCyc:MONOMER-14557.
BRENDA4.4.1.21. 700.
SABIO-RKO34667.

Family and domain databases

Gene3D3.30.1360.80. 1 hit.
HAMAPMF_00091. LuxS.
InterProIPR011249. Metalloenz_LuxS/M16.
IPR003815. S-ribosylhomocysteinase.
[Graphical view]
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]
SUPFAMSSF63411. SSF63411. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO34667.
PROO34667.

Entry information

Entry nameLUXS_BACSU
AccessionPrimary (citable) accession number: O34667
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList