LUXS_ECOLI
ID LUXS_ECOLI Reviewed; 171 AA.
AC P45578; P77134; P77805;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 168.
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; Synonyms=ygaG; OrderedLocusNames=b2687, JW2662;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-76.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 53-171.
RX PubMed=1409590; DOI=10.1073/pnas.89.19.8938;
RA Lomovskaya O., Lewis K.;
RT "Emr, an Escherichia coli locus for multidrug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:8938-8942(1992).
RN [6]
RP PROTEIN SEQUENCE OF 2-10.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP IDENTIFICATION.
RX PubMed=7567469; DOI=10.1093/nar/23.17.3554;
RA Borodovsky M., McIninch J., Koonin E.V., Rudd K.E., Medigue C., Danchin A.;
RT "Detection of new genes in a bacterial genome using Markov models for three
RT gene classes.";
RL Nucleic Acids Res. 23:3554-3562(1995).
RN [8]
RP FUNCTION.
RX PubMed=9618536; DOI=10.1073/pnas.95.12.7046;
RA Surette M.G., Bassler B.L.;
RT "Quorum sensing in Escherichia coli and Salmonella typhimurium.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:7046-7050(1998).
RN [9]
RP FUNCTION.
RX PubMed=9990077; DOI=10.1073/pnas.96.4.1639;
RA Surette M.G., Miller M.B., Bassler B.L.;
RT "Quorum sensing in Escherichia coli, Salmonella typhimurium, and Vibrio
RT harveyi: a new family of genes responsible for autoinducer production.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:1639-1644(1999).
CC -!- FUNCTION: Involved in the synthesis of autoinducer 2 (AI-2) which is
CC secreted by bacteria and is used to communicate both the cell density
CC and the metabolic potential of the environment. The regulation of gene
CC expression in response to changes in cell density is called quorum
CC sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to
CC homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).
CC {ECO:0000269|PubMed:9618536, ECO:0000269|PubMed:9990077}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = (S)-4,5-
CC dihydroxypentane-2,3-dione + L-homocysteine; Xref=Rhea:RHEA:17753,
CC ChEBI:CHEBI:29484, ChEBI:CHEBI:58195, ChEBI:CHEBI:58199; EC=4.4.1.21;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INTERACTION:
CC P45578; P0A6Y8: dnaK; NbExp=2; IntAct=EBI-562313, EBI-542092;
CC -!- MISCELLANEOUS: E.coli strain DH5-alpha does not make AI-2; it has a
CC frameshift mutation in the luxS gene that disrupts the protein coding
CC region.
CC -!- SIMILARITY: Belongs to the LuxS family. {ECO:0000305}.
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DR EMBL; U00096; AAC75734.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16549.1; -; Genomic_DNA.
DR EMBL; U83186; AAB40286.1; -; Genomic_DNA.
DR EMBL; M86657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; H65048; H65048.
DR RefSeq; NP_417172.1; NC_000913.3.
DR RefSeq; WP_001130211.1; NZ_SSZK01000020.1.
DR AlphaFoldDB; P45578; -.
DR SMR; P45578; -.
DR BioGRID; 4263180; 19.
DR DIP; DIP-10131N; -.
DR IntAct; P45578; 5.
DR STRING; 511145.b2687; -.
DR BindingDB; P45578; -.
DR ChEMBL; CHEMBL3496; -.
DR SWISS-2DPAGE; P45578; -.
DR jPOST; P45578; -.
DR PaxDb; P45578; -.
DR PRIDE; P45578; -.
DR EnsemblBacteria; AAC75734; AAC75734; b2687.
DR EnsemblBacteria; BAA16549; BAA16549; BAA16549.
DR GeneID; 66673444; -.
DR GeneID; 947168; -.
DR KEGG; ecj:JW2662; -.
DR KEGG; eco:b2687; -.
DR PATRIC; fig|1411691.4.peg.4052; -.
DR EchoBASE; EB2573; -.
DR eggNOG; COG1854; Bacteria.
DR HOGENOM; CLU_107531_2_0_6; -.
DR InParanoid; P45578; -.
DR OMA; GPMGCLT; -.
DR PhylomeDB; P45578; -.
DR BioCyc; EcoCyc:EG12712-MON; -.
DR BioCyc; MetaCyc:EG12712-MON; -.
DR BRENDA; 4.4.1.21; 2026.
DR SABIO-RK; P45578; -.
DR PRO; PR:P45578; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0043768; F:S-ribosylhomocysteine lyase activity; IDA:EcoCyc.
DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IDA:EcoCyc.
DR GO; GO:0009372; P:quorum sensing; IMP:EcoCyc.
DR Gene3D; 3.30.1360.80; -; 1.
DR HAMAP; MF_00091; LuxS; 1.
DR InterPro; IPR037005; LuxS_sf.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR003815; S-ribosylhomocysteinase.
DR PANTHER; PTHR35799; PTHR35799; 1.
DR Pfam; PF02664; LuxS; 1.
DR PIRSF; PIRSF006160; AI2; 1.
DR PRINTS; PR01487; LUXSPROTEIN.
DR SUPFAM; SSF63411; SSF63411; 1.
PE 1: Evidence at protein level;
KW Autoinducer synthesis; Direct protein sequencing; Iron; Lyase;
KW Metal-binding; Quorum sensing; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 2..171
FT /note="S-ribosylhomocysteine lyase"
FT /id="PRO_0000172220"
FT BINDING 54
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CONFLICT 31
FT /note="D -> E (in Ref. 4; AAB40286)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 171 AA; 19416 MW; 131F57F1866DA105 CRC64;
MPLLDSFTVD HTRMEAPAVR VAKTMNTPHG DAITVFDLRF CVPNKEVMPE RGIHTLEHLF
AGFMRNHLNG NGVEIIDISP MGCRTGFYMS LIGTPDEQRV ADAWKAAMED VLKVQDQNQI
PELNVYQCGT YQMHSLQEAQ DIARSILERD VRINSNEELA LPKEKLQELH I
