AHLL_BACCE
ID AHLL_BACCE Reviewed; 250 AA.
AC Q08GP4;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=N-acyl homoserine lactonase {ECO:0000303|PubMed:16972128};
DE Short=AHL-lactonase {ECO:0000303|PubMed:16972128};
DE EC=3.1.1.81;
DE AltName: Full=Quorum-quenching N-acyl-homoserine lactonase {ECO:0000312|EMBL:CAJ84442.1};
GN Name=Y2-aiiA {ECO:0000312|EMBL:CAJ84442.1};
OS Bacillus cereus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1396;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAJ84442.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND MUTAGENESIS OF
RP TYR-194.
RC STRAIN=Y2 {ECO:0000312|EMBL:CAJ84442.1};
RX PubMed=16972128; DOI=10.1007/s00284-006-0224-1;
RA Lu X., Yuan Y., Xue X.L., Zhang G.P., Zhou S.N.;
RT "Identification of the critical role of Tyr-194 in the catalytic activity
RT of a novel N-acyl-homoserine lactonase from marine Bacillus cereus strain
RT Y2.";
RL Curr. Microbiol. 53:346-350(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine
CC + H(+); Xref=Rhea:RHEA:22576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:55474, ChEBI:CHEBI:58921; EC=3.1.1.81;
CC Evidence={ECO:0000269|PubMed:16972128};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q7B8B9};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q7B8B9};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q7B8B9}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC {ECO:0000305}.
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DR EMBL; AM235210; CAJ84442.1; -; Genomic_DNA.
DR AlphaFoldDB; Q08GP4; -.
DR SMR; Q08GP4; -.
DR STRING; 1396.DJ87_1487; -.
DR eggNOG; COG0491; Bacteria.
DR GO; GO:0102007; F:acyl-L-homoserine-lactone lactonohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..250
FT /note="N-acyl homoserine lactonase"
FT /id="PRO_0000403298"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT MUTAGEN 194
FT /note="Y->A: Activity decreases significantly."
FT /evidence="ECO:0000269|PubMed:16972128"
SQ SEQUENCE 250 AA; 28191 MW; 1915E4DCA5A39301 CRC64;
MTVKKLYFVP AGRCMLDRSS VNSTLTPGNL LNLPVWCYLL ETEEGPILVD TGMPESAVHN
ENLFEGTFAE GQILPKMTEE DRIVTILKRV GYKPEDLLYI ISSHLHFDHA GGNGAFSNTP
IIIQRAEYEA AQYREEYLKE CILPNLNYKI IEGDYEVVPG VQLLYTPGHS PGHQSLLIET
EKSGLVLLTI DASYTKENFE DEVPFAGFDS ELALSSIKRL KEVVMKEKPI VFFGHDIEQE
KGCKVFPEYI
