Reviewed, UniProtKB/Swiss-Prot B6I678 (LUXS_ECOSE)

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:	ECSE_2940

Organism

Escherichia coli (strain SE11) [Complete proteome] [HAMAP]

Taxonomic identifier

409438 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	171 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
Subunit structure	Homodimer By similarity.
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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 171	171	S-ribosylhomocysteine lyase HAMAP MF_00091		PRO_1000093306
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)
	B6I678-1 [UniParc]. Last modified December 16, 2008. Version 1. Checksum: 1EA957F1866DA105	FASTA	171	19,417
	10 20 30 40 50 60 MPLLDSFTVD HTRMEAPAVR VAKTMNTPHG DAITVFDLRF CVPNKEVMPE RGIHTLEHLF 70 80 90 100 110 120 AGFMRNHLNG NGVEIIDISP MGCRTGFYMS LIGTPDEQRV ADAWKAAMED VLKVQDQNQI 130 140 150 160 170 PELNVYQCGT YQMHSLQEAQ DIARSILERD VRINSNEELA LPEEKLQELH I

References

[1]

"Complete genome sequence and comparative analysis of the wild-type commensal Escherichia coli strain SE11 isolated from a healthy adult." Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T., Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M. DNA Res. 15:375-386(2008) [PubMed: 18931093] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AP009240 Genomic DNA. Translation: BAG78464.1.
RefSeq	YP_002294215.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	7001325.
GenomeReviews	Gene locus ECSE_2940 in contig AP009240_GR.
KEGG	ecy:ECSE_2940.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	VRIAKTM.
Family and domain databases
HAMAP	MF_00091. [Tree]
InterPro	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.
ProtoNet	Search...

Entry information

Entry name

LUXS_ECOSE

Accession

Primary (citable) accession number: B6I678

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	December 16, 2008
Last modified:	November 3, 2009
This is version 8 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)