Reviewed, UniProtKB/Swiss-Prot Q9PN97 (LUXS_CAMJE)

Names and origin

Protein names

Recommended 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:	Cj1198

Organism

Campylobacter jejuni [Complete proteome] [HAMAP]

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
Gene Ontology (GO)
Biological process	quorum sensing Inferred from electronic annotation. Source: HAMAP
Molecular function	S-ribosylhomocysteine lyase activity Inferred from electronic annotation. Source: HAMAP iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
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

	Sequence		Length	Mass (Da)
	Q9PN97-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 717CEADF980E1EC1	FASTA	164	18,209
	10 20 30 40 50 60 MPLLDSFKVD HTKMPAPAVR LAKVMKTPKG DDISVFDLRF CIPNKDIMSE KGTHTLEHLF 70 80 90 100 110 120 AGFMRDHLNS NSVEIIDISP MGCRTGFYMS LIGTPDEKSI AKAWEAAMKD VLSVSDQSKI 130 140 150 160 PELNIYQCGT CAMHSLDEAK QIAQKVLNLG ISIINNKELK LENA

References

	« Hide 'large scale' referencesShow '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. , van Vliet A.H.M., Whitehead S., 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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL111168 Genomic DNA. Translation: CAL35313.1.
PIR	H81325.
RefSeq	YP_002344589.1.
3D structure databases
SMR	Q9PN97. Positions 3-163.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9PN97. 32 interactions.
Genome annotation databases
GeneID	905488.
GenomeReviews	Gene locus Cj1198 in contig AL111168_GR.
KEGG	cje:Cj1198.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG347473.
OMA	VRIAKTM.
Enzyme and pathway databases
BioCyc	CJEJ192222:CJ1198-MONOMER.
BRENDA	4.4.1.21. 255835.
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.
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]
ProtoNet	Search...

Entry information

Entry name

LUXS_CAMJE

Accession

Primary (citable) accession number: Q9PN97
Secondary accession number(s): Q0P958

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	October 1, 2000
Last modified:	January 19, 2010
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)