LUXS_BACSU
ID LUXS_BACSU Reviewed; 157 AA.
AC O34667;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 145.
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=ytjB; OrderedLocusNames=BSU30670;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP COFACTOR, CHARACTERIZATION, AND MUTAGENESIS OF GLU-57 AND CYS-84.
RX PubMed=12705835; DOI=10.1021/bi034289j;
RA Zhu J., Dizin E., Hu X., Wavreille A.-S., Park J., Pei D.;
RT "S-ribosylhomocysteinase (LuxS) is a mononuclear iron protein.";
RL Biochemistry 42:4717-4726(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS).
RX PubMed=11601850; DOI=10.1006/jmbi.2001.5027;
RA Ruzheinikov S.N., Das S.K., Sedelnikova S.E., Hartley A., Foster S.J.,
RA Horsburgh M.J., Cox A.G., McCleod C.W., Mekhalfia A., Blackburn G.M.,
RA Rice D.W., Baker P.J.;
RT "The 1.2 A structure of a novel quorum-sensing protein, Bacillus subtilis
RT LuxS.";
RL J. Mol. Biol. 313:111-122(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX PubMed=11553770; DOI=10.1073/pnas.191223098;
RA Hilgers M.T., Ludwig M.L.;
RT "Crystal structure of the quorum-sensing protein LuxS reveals a catalytic
RT metal site.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:11169-11174(2001).
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 -!- 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;
CC Evidence={ECO:0000269|PubMed:12705835};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000269|PubMed:12705835};
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the LuxS family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF008220; AAC00235.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15045.1; -; Genomic_DNA.
DR PIR; A69994; A69994.
DR RefSeq; NP_390945.1; NC_000964.3.
DR RefSeq; WP_003219361.1; NZ_JNCM01000036.1.
DR PDB; 1IE0; X-ray; 1.60 A; A=1-157.
DR PDB; 1J98; X-ray; 1.20 A; A=1-157.
DR PDB; 1JQW; X-ray; 2.30 A; A=1-157.
DR PDB; 1JVI; X-ray; 2.20 A; A=1-157.
DR PDB; 1YCL; X-ray; 1.80 A; A=2-157.
DR PDB; 2FQO; X-ray; 1.87 A; A=1-157.
DR PDB; 2FQT; X-ray; 1.79 A; A=1-157.
DR PDBsum; 1IE0; -.
DR PDBsum; 1J98; -.
DR PDBsum; 1JQW; -.
DR PDBsum; 1JVI; -.
DR PDBsum; 1YCL; -.
DR PDBsum; 2FQO; -.
DR PDBsum; 2FQT; -.
DR AlphaFoldDB; O34667; -.
DR SMR; O34667; -.
DR STRING; 224308.BSU30670; -.
DR BindingDB; O34667; -.
DR ChEMBL; CHEMBL5171; -.
DR DrugBank; DB04182; (S)-2-Amino-4-[(2s,3r)-2,3,5-Trihydroxy-4-Oxo-Pentyl]Mercapto-Butyric Acid.
DR DrugBank; DB02321; 5-(3-Amino-4,4-Dihyroxy-Butylsulfanylmethyl)-Tetrahydro-Furan-2,3,4-Triol.
DR DrugBank; DB04422; Homocysteine.
DR DrugBank; DB03661; L-cysteic acid.
DR DrugCentral; O34667; -.
DR jPOST; O34667; -.
DR PaxDb; O34667; -.
DR PRIDE; O34667; -.
DR EnsemblBacteria; CAB15045; CAB15045; BSU_30670.
DR GeneID; 64304786; -.
DR GeneID; 937106; -.
DR KEGG; bsu:BSU30670; -.
DR PATRIC; fig|224308.179.peg.3325; -.
DR eggNOG; COG1854; Bacteria.
DR InParanoid; O34667; -.
DR OMA; GPMGCLT; -.
DR PhylomeDB; O34667; -.
DR BioCyc; BSUB:BSU30670-MON; -.
DR BioCyc; MetaCyc:MON-14557; -.
DR BRENDA; 4.4.1.21; 658.
DR SABIO-RK; O34667; -.
DR EvolutionaryTrace; O34667; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0043768; F:S-ribosylhomocysteine lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009372; P:quorum sensing; IEA:UniProtKB-UniRule.
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 3D-structure; Autoinducer synthesis; Iron; Lyase; Metal-binding;
KW Quorum sensing; Reference proteome.
FT CHAIN 1..157
FT /note="S-ribosylhomocysteine lyase"
FT /id="PRO_0000172211"
FT BINDING 54
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 58
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 126
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT MUTAGEN 57
FT /note="E->A,Q: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:12705835"
FT MUTAGEN 57
FT /note="E->D: 220-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:12705835"
FT MUTAGEN 84
FT /note="C->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:12705835"
FT MUTAGEN 84
FT /note="C->D,S: Almost complete loss of activity."
FT /evidence="ECO:0000269|PubMed:12705835"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:1J98"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:1J98"
FT STRAND 16..27
FT /evidence="ECO:0007829|PDB:1J98"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:1J98"
FT STRAND 31..39
FT /evidence="ECO:0007829|PDB:1J98"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:1J98"
FT HELIX 50..68
FT /evidence="ECO:0007829|PDB:1J98"
FT STRAND 72..81
FT /evidence="ECO:0007829|PDB:1J98"
FT STRAND 85..94
FT /evidence="ECO:0007829|PDB:1J98"
FT HELIX 98..112
FT /evidence="ECO:0007829|PDB:1J98"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:1J98"
FT TURN 127..130
FT /evidence="ECO:0007829|PDB:1J98"
FT HELIX 134..145
FT /evidence="ECO:0007829|PDB:1J98"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:1J98"
SQ SEQUENCE 157 AA; 17714 MW; DD011A2A88BD2FFB CRC64;
MPSVESFELD HNAVVAPYVR HCGVHKVGTD GVVNKFDIRF CQPNKQAMKP DTIHTLEHLL
AFTIRSHAEK YDHFDIIDIS PMGCQTGYYL VVSGEPTSAE IVDLLEDTMK EAVEITEIPA
ANEKQCGQAK LHDLEGAKRL MRFWLSQDKE ELLKVFG
