LUXS_HALH3
ID LUXS_HALH3 Reviewed; 152 AA.
AC I0JJR3; A1DZZ4;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 51.
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=HBHAL_2021;
OS Halobacillus halophilus (strain ATCC 35676 / DSM 2266 / JCM 20832 / KCTC
OS 3685 / LMG 17431 / NBRC 102448 / NCIMB 2269) (Sporosarcina halophila).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=866895;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / KCTC 3685 / LMG 17431 / NBRC
RC 102448 / NCIMB 2269;
RX PubMed=17085700; DOI=10.1128/aem.01625-06;
RA Sewald X., Saum S.H., Palm P., Pfeiffer F., Oesterhelt D., Mueller V.;
RT "Autoinducer-2-producing protein LuxS, a novel salt- and chloride-induced
RT protein in the moderately halophilic bacterium Halobacillus halophilus.";
RL Appl. Environ. Microbiol. 73:371-379(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / KCTC 3685 / LMG 17431 / NBRC
RC 102448 / NCIMB 2269;
RX PubMed=22583374; DOI=10.1111/j.1462-2920.2012.02770.x;
RA Saum S.H., Pfeiffer F., Palm P., Rampp M., Schuster S.C., Muller V.,
RA Oesterhelt D.;
RT "Chloride and organic osmolytes: a hybrid strategy to cope with elevated
RT salinities by the moderately halophilic, chloride-dependent bacterium
RT Halobacillus halophilus.";
RL Environ. Microbiol. 15:1619-1633(2013).
RN [3]
RP PROTEIN SEQUENCE OF 1-19, AND INDUCTION.
RC STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / KCTC 3685 / LMG 17431 / NBRC
RC 102448 / NCIMB 2269;
RX PubMed=12399491; DOI=10.1128/jb.184.22.6207-6215.2002;
RA Roessler M., Muller V.;
RT "Chloride, a new environmental signal molecule involved in gene regulation
RT in a moderately halophilic bacterium, Halobacillus halophilus.";
RL J. Bacteriol. 184:6207-6215(2002).
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) (By
CC similarity). {ECO:0000250}.
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 -!- INDUCTION: Expression is growth phase-dependent, with maximal
CC expression in the mid-exponential growth phase. Induced by high salt
CC concentrations (at protein level). {ECO:0000269|PubMed:12399491,
CC ECO:0000269|PubMed:17085700}.
CC -!- SIMILARITY: Belongs to the LuxS family. {ECO:0000305}.
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DR EMBL; EF088802; ABL09514.1; -; Genomic_DNA.
DR EMBL; HE717023; CCG44382.1; -; Genomic_DNA.
DR RefSeq; WP_014642285.1; NC_017668.1.
DR AlphaFoldDB; I0JJR3; -.
DR SMR; I0JJR3; -.
DR STRING; 866895.HBHAL_2021; -.
DR EnsemblBacteria; CCG44382; CCG44382; HBHAL_2021.
DR KEGG; hhd:HBHAL_2021; -.
DR PATRIC; fig|866895.3.peg.1028; -.
DR eggNOG; COG1854; Bacteria.
DR HOGENOM; CLU_107531_2_0_9; -.
DR OrthoDB; 1779617at2; -.
DR Proteomes; UP000007397; 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 Autoinducer synthesis; Direct protein sequencing; Iron; Lyase;
KW Metal-binding; Quorum sensing; Reference proteome.
FT CHAIN 1..152
FT /note="S-ribosylhomocysteine lyase"
FT /id="PRO_0000429001"
FT BINDING 56
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CONFLICT 2
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 8
FT /note="S -> V (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 152 AA; 17301 MW; A90DD98BD0C0BFF6 CRC64;
MTQMNVESFN LDHTKVKAPY IRLVGVTEGD KGDKIYKYDI RVKQPNQEHM DMPALHSLEH
LMAENSRNHH DRIIDIGPMG CQTGFYLAVL NDDSYENILQ VVENTLKDVL NATEVPACNE
VQCGFAASHS LEGAQELARE LLNKRNEWTE VF
