P0C0C7 (LUXS_STRPY) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 34.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: S-ribosylhomocysteine lyase EC=4.4.1.21 Alternative name(s): AI-2 synthesis protein Autoinducer-2 production protein LuxS | ||
| Gene names |
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| Organism | Streptococcus pyogenes | ||
| Taxonomic identifier | 1314 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus![]() |
Protein attributes
| Sequence length | 160 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred 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-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 By similarity. HAMAP-Rule MF_00091 |
| Subunit structure | Homodimer By similarity. HAMAP-Rule MF_00091 |
| Sequence similarities | Belongs to the LuxS family. |
| Sequence caution | The sequence AAG28749.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Autoinducer synthesis Quorum sensing |
| Ligand | Iron Metal-binding |
| Molecular function | Lyase |
| Gene Ontology (GO) | |
| Biological_process | metabolic process Inferred from electronic annotation. Source: GOC quorum sensingInferred from electronic annotation. Source: HAMAP |
| Molecular_function | S-ribosylhomocysteine lyase activity Inferred from electronic annotation. Source: HAMAP iron ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 160 | 160 | S-ribosylhomocysteine lyase HAMAP-Rule MF_00091 | PRO_0000172267 | |||||
Sites | |||||||||
| Metal binding | 57 | 1 | Iron By similarity | ||||||
| Metal binding | 61 | 1 | Iron By similarity | ||||||
| Metal binding | 127 | 1 | Iron By similarity | ||||||
Sequences
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References
| [1] | "Mutation of luxS affects growth and virulence factor expression in Streptococcus pyogenes." Lyon W.R., Madden J.C., Levin J.C., Stein J.L., Caparon M.G. Mol. Microbiol. 42:145-157(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF295118 Genomic DNA. Translation: AAG28749.1. Different initiation. |
3D structure databases | |
| ProteinModelPortal | P0C0C7. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| eggNOG | COG1854. |
Family and domain databases | |
| Gene3D | 3.30.1360.80. 1 hit. |
| HAMAP | MF_00091. LuxS. |
| InterPro | IPR011249. Metalloenz_LuxS/M16. IPR003815. S-ribosylhomocysteinase. [Graphical view] |
| Pfam | PF02664. LuxS. 1 hit. [Graphical view] |
| PIRSF | PIRSF006160. AI2. 1 hit. |
| PRINTS | PR01487. LUXSPROTEIN. |
| ProDom | PD013172. S-ribosylhomocysteinase. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SUPFAM | SSF63411. Metalloenz_metal-bd. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | LUXS_STRPY | ||||||||
| Accession | Primary (citable) accession number: P0C0C7 Secondary accession number(s): P0A3P7, Q99YL7, Q9EVB4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
