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O34667

- LUXS_BACSU

UniProt

O34667 - LUXS_BACSU

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Protein
S-ribosylhomocysteine lyase
Gene
luxS, ytjB, BSU30670
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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).UniRule annotation

Catalytic activityi

S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione.UniRule annotation

Cofactori

Binds 1 iron ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi54 – 541Iron
Metal bindingi58 – 581Iron
Metal bindingi126 – 1261Iron

GO - Molecular functioni

  1. S-ribosylhomocysteine lyase activity Source: UniProtKB-HAMAP
  2. iron ion binding Source: InterPro

GO - Biological processi

  1. quorum sensing Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Autoinducer synthesis, Quorum sensing

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciBSUB:BSU30670-MONOMER.
MetaCyc:MONOMER-14557.
BRENDAi4.4.1.21. 700.
SABIO-RKO34667.

Names & Taxonomyi

Protein namesi
Recommended name:
S-ribosylhomocysteine lyase (EC:4.4.1.21)
Alternative name(s):
AI-2 synthesis protein
Autoinducer-2 production protein LuxS
Gene namesi
Name:luxS
Synonyms:ytjB
Ordered Locus Names:BSU30670
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU30670. [Micado]

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi57 – 571E → A or Q: Complete loss of activity. 1 Publication
Mutagenesisi57 – 571E → D: 220-fold decrease in activity. 1 Publication
Mutagenesisi84 – 841C → A: Complete loss of activity. 1 Publication
Mutagenesisi84 – 841C → D or S: Almost complete loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 157157S-ribosylhomocysteine lyaseUniRule annotation
PRO_0000172211Add
BLAST

Proteomic databases

PaxDbiO34667.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi224308.BSU30670.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 84
Turni11 – 133
Beta strandi16 – 2712
Turni28 – 303
Beta strandi31 – 399
Turni43 – 453
Helixi50 – 6819
Beta strandi72 – 8110
Beta strandi85 – 9410
Helixi98 – 11215
Turni123 – 1253
Turni127 – 1304
Helixi134 – 14512
Helixi149 – 1524

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IE0X-ray1.60A1-157[»]
1J98X-ray1.20A1-157[»]
1JQWX-ray2.30A1-157[»]
1JVIX-ray2.20A1-157[»]
1YCLX-ray1.80A2-157[»]
2FQOX-ray1.87A1-157[»]
2FQTX-ray1.79A1-157[»]
ProteinModelPortaliO34667.
SMRiO34667. Positions 4-157.

Miscellaneous databases

EvolutionaryTraceiO34667.

Family & Domainsi

Sequence similaritiesi

Belongs to the LuxS family.

Phylogenomic databases

eggNOGiCOG1854.
HOGENOMiHOG000040372.
KOiK07173.
OMAiEFRAVIW.
OrthoDBiEOG68WRBM.
PhylomeDBiO34667.

Family and domain databases

Gene3Di3.30.1360.80. 1 hit.
HAMAPiMF_00091. LuxS.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR003815. S-ribosylhomocysteinase.
[Graphical view]
PfamiPF02664. LuxS. 1 hit.
[Graphical view]
PIRSFiPIRSF006160. AI2. 1 hit.
PRINTSiPR01487. LUXSPROTEIN.
ProDomiPD013172. S-ribosylhomocysteinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF63411. SSF63411. 1 hit.

Sequencei

Sequence statusi: Complete.

O34667-1 [UniParc]FASTAAdd to Basket

« Hide

MPSVESFELD HNAVVAPYVR HCGVHKVGTD GVVNKFDIRF CQPNKQAMKP    50
DTIHTLEHLL AFTIRSHAEK YDHFDIIDIS PMGCQTGYYL VVSGEPTSAE 100
IVDLLEDTMK EAVEITEIPA ANEKQCGQAK LHDLEGAKRL MRFWLSQDKE 150
ELLKVFG 157
Length:157
Mass (Da):17,714
Last modified:January 1, 1998 - v1
Checksum:iDD011A2A88BD2FFB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF008220 Genomic DNA. Translation: AAC00235.1.
AL009126 Genomic DNA. Translation: CAB15045.1.
PIRiA69994.
RefSeqiNP_390945.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB15045; CAB15045; BSU30670.
GeneIDi937106.
KEGGibsu:BSU30670.
PATRICi18978038. VBIBacSub10457_3207.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF008220 Genomic DNA. Translation: AAC00235.1 .
AL009126 Genomic DNA. Translation: CAB15045.1 .
PIRi A69994.
RefSeqi NP_390945.1. NC_000964.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IE0 X-ray 1.60 A 1-157 [» ]
1J98 X-ray 1.20 A 1-157 [» ]
1JQW X-ray 2.30 A 1-157 [» ]
1JVI X-ray 2.20 A 1-157 [» ]
1YCL X-ray 1.80 A 2-157 [» ]
2FQO X-ray 1.87 A 1-157 [» ]
2FQT X-ray 1.79 A 1-157 [» ]
ProteinModelPortali O34667.
SMRi O34667. Positions 4-157.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU30670.

Chemistry

BindingDBi O34667.
ChEMBLi CHEMBL5171.

Proteomic databases

PaxDbi O34667.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB15045 ; CAB15045 ; BSU30670 .
GeneIDi 937106.
KEGGi bsu:BSU30670.
PATRICi 18978038. VBIBacSub10457_3207.

Organism-specific databases

GenoListi BSU30670. [Micado ]

Phylogenomic databases

eggNOGi COG1854.
HOGENOMi HOG000040372.
KOi K07173.
OMAi EFRAVIW.
OrthoDBi EOG68WRBM.
PhylomeDBi O34667.

Enzyme and pathway databases

BioCyci BSUB:BSU30670-MONOMER.
MetaCyc:MONOMER-14557.
BRENDAi 4.4.1.21. 700.
SABIO-RK O34667.

Miscellaneous databases

EvolutionaryTracei O34667.
PROi O34667.

Family and domain databases

Gene3Di 3.30.1360.80. 1 hit.
HAMAPi MF_00091. LuxS.
InterProi IPR011249. Metalloenz_LuxS/M16.
IPR003815. S-ribosylhomocysteinase.
[Graphical view ]
Pfami PF02664. LuxS. 1 hit.
[Graphical view ]
PIRSFi PIRSF006160. AI2. 1 hit.
PRINTSi PR01487. LUXSPROTEIN.
ProDomi PD013172. S-ribosylhomocysteinase. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF63411. SSF63411. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region."
    Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.
    Microbiology 143:3431-3441(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "S-ribosylhomocysteinase (LuxS) is a mononuclear iron protein."
    Zhu J., Dizin E., Hu X., Wavreille A.-S., Park J., Pei D.
    Biochemistry 42:4717-4726(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR, CHARACTERIZATION, MUTAGENESIS OF GLU-57 AND CYS-84.
  4. Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS).
  5. "Crystal structure of the quorum-sensing protein LuxS reveals a catalytic metal site."
    Hilgers M.T., Ludwig M.L.
    Proc. Natl. Acad. Sci. U.S.A. 98:11169-11174(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).

Entry informationi

Entry nameiLUXS_BACSU
AccessioniPrimary (citable) accession number: O34667
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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