Q9PN97 (LUXS_CAMJE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 63.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·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 | Campylobacter jejuni | ||||
| Taxonomic identifier | 197 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter |
Protein attributes
| Sequence length | 164 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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). Ref.2 |
| 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 process | Autoinducer synthesis Quorum sensing |
| Ligand | Iron Metal-binding |
| Molecular function | Lyase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | quorum sensing Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | S-ribosylhomocysteine lyase activity Inferred from electronic annotation. Source: EC iron ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| fliG | Q0PBJ0 | 1 | EBI-1192597,EBI-1191336 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 164 | 164 | S-ribosylhomocysteine lyase HAMAP MF_00091 | PRO_0000172214 | |||||
Sites | |||||||||
| Metal binding | 54 | 1 | Iron By similarity | ||||||
| Metal binding | 58 | 1 | Iron By similarity | ||||||
| Metal binding | 128 | 1 | Iron By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. Barrell B.G.Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2. |
| [2] | "Quorum sensing in Campylobacter jejuni: detection of a luxS encoded signalling molecule." Elvers K.T., Park S.F. Microbiology 148:1475-1481(2002) [PubMed: 11988522] [Abstract] Cited for: FUNCTION. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AL111168 Genomic DNA. Translation: CAL35313.1. |
| PIR | H81325. |
| RefSeq | YP_002344589.1. NC_002163.1. |
3D structure databases | |
| ProteinModelPortal | Q9PN97. |
| SMR | Q9PN97. Positions 3-163. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q9PN97. 32 interactions. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 905488. |
| GenomeReviews | Gene locus Cj1198 in contig AL111168_GR. |
| KEGG | cje:Cj1198. |
| PATRIC | 20059352. VBICamJej33762_1179. |
Phylogenomic databases | |
| HOGENOM | HBG347473. |
| OMA | PHGDTIT. |
| ProtClustDB | PRK02260. |
Enzyme and pathway databases | |
| BioCyc | CJEJ192222:CJ1198-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00091. LuxS. [Tree] |
| InterPro | IPR011249. Metalloenz_metal-bd. IPR003815. S-ribosylhomocysteinase. [Graphical view] |
| Gene3D | G3DSA:3.30.1360.80. S-ribosylhomocysteinase. 1 hit. |
| KO | K07173. |
| 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_CAMJE | ||||||||
| Accession | Primary (citable) accession number: Q9PN97 Secondary accession number(s): Q0P958 | ||||||||
| 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 |

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