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Database: UniProt/SWISS-PROT
Entry: LUXS_LACJO
LinkDB: LUXS_LACJO
Original site: LUXS_LACJO 
ID   LUXS_LACJO              Reviewed;         158 AA.
AC   Q74HV0;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   14-MAY-2014, entry version 64.
DE   RecName: Full=S-ribosylhomocysteine lyase;
DE            EC=4.4.1.21;
DE   AltName: Full=AI-2 synthesis protein;
DE   AltName: Full=Autoinducer-2 production protein LuxS;
GN   Name=luxS; OrderedLocusNames=LJ_0631;
OS   Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=257314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNCM I-1225 / La1 / NCC 533;
RX   PubMed=14983040; DOI=10.1073/pnas.0307327101;
RA   Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C.,
RA   Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R.,
RA   Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.;
RT   "The genome sequence of the probiotic intestinal bacterium
RT   Lactobacillus johnsonii NCC 533.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004).
CC   -!- FUNCTION: Involved in the synthesis of autoinducer 2 (AI-2) which
CC       is secreted by bacteria and is used to communicate both the cell
CC       density and the metabolic potential of the environment. The
CC       regulation of gene expression in response to changes in cell
CC       density is called quorum sensing. Catalyzes the transformation of
CC       S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-
CC       dihydroxy-2,3-pentadione (DPD) (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-
CC       homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione.
CC   -!- COFACTOR: Binds 1 iron ion per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the LuxS family.
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DR   EMBL; AE017198; AAS09590.1; -; Genomic_DNA.
DR   RefSeq; NP_965624.1; NC_005362.1.
DR   ProteinModelPortal; Q74HV0; -.
DR   STRING; 257314.LJ0631; -.
DR   EnsemblBacteria; AAS09590; AAS09590; LJ_0631.
DR   GeneID; 2743085; -.
DR   KEGG; ljo:LJ0631; -.
DR   PATRIC; 22240057; VBILacJoh1832_1644.
DR   eggNOG; COG1854; -.
DR   KO; K07173; -.
DR   OMA; RDHLNSD; -.
DR   OrthoDB; EOG68WRBM; -.
DR   BioCyc; LJOH257314:GJN3-1695-MONOMER; -.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0043768; F:S-ribosylhomocysteine lyase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009372; P:quorum sensing; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.30.1360.80; -; 1.
DR   HAMAP; MF_00091; LuxS; 1.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR003815; S-ribosylhomocysteinase.
DR   Pfam; PF02664; LuxS; 1.
DR   PIRSF; PIRSF006160; AI2; 1.
DR   PRINTS; PR01487; LUXSPROTEIN.
DR   ProDom; PD013172; S-ribosylhomocysteinase; 1.
DR   SUPFAM; SSF63411; SSF63411; 1.
PE   3: Inferred from homology;
KW   Autoinducer synthesis; Complete proteome; Iron; Lyase; Metal-binding;
KW   Quorum sensing.
FT   CHAIN         1    158       S-ribosylhomocysteine lyase.
FT                                /FTId=PRO_0000172231.
FT   METAL        54     54       Iron (By similarity).
FT   METAL        58     58       Iron (By similarity).
FT   METAL       124    124       Iron (By similarity).
SQ   SEQUENCE   158 AA;  17795 MW;  D5B0B6C088F9DAF3 CRC64;
     MGKVESFELD HTKVKAPYVR LITVEEGQKG DKISNFDLRL VQPNENAIPT GGLHTIEHLL
     AGLLRDRIDG YIDCSPFGCR TGFHLLVWGT PSTTDVAKAL KESLEEIRDN ITWEDVPGTT
     IESCGNYRDH SLFSAKQWSR DILEKGISDD PFERHVVE
//
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