AHLL_BACSP
ID AHLL_BACSP Reviewed; 250 AA.
AC Q9L8R8;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=N-acyl homoserine lactonase {ECO:0000250|UniProtKB:Q7B8B9};
DE Short=AHL-lactonase {ECO:0000303|PubMed:11459062, ECO:0000303|PubMed:14734559};
DE Short=Acyl-homoserine lactonase {ECO:0000303|PubMed:11459062};
DE EC=3.1.1.81;
GN Name=aiiA {ECO:0000312|EMBL:AAF62398.1};
OS Bacillus sp.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1409;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF62398.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND MUTAGENESIS OF
RP HIS-104; HIS-106; ASP-108; HIS-109 AND HIS-169.
RC STRAIN=240B1 {ECO:0000312|EMBL:AAF62398.1};
RX PubMed=10716724; DOI=10.1073/pnas.97.7.3526;
RA Dong Y.H., Xu J.L., Li X.Z., Zhang L.H.;
RT "AiiA, an enzyme that inactivates the acylhomoserine lactone quorum-sensing
RT signal and attenuates the virulence of Erwinia carotovora.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3526-3531(2000).
RN [2] {ECO:0000305}
RP CATALYTIC ACTIVITY.
RX PubMed=11459062; DOI=10.1038/35081101;
RA Dong Y.H., Wang L.H., Xu J.L., Zhang H.B., Zhang X.F., Zhang L.H.;
RT "Quenching quorum-sensing-dependent bacterial infection by an N-acyl
RT homoserine lactonase.";
RL Nature 411:813-817(2001).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND MUTAGENESIS OF HIS-106; ASP-108; HIS-109 AND HIS-169.
RX PubMed=14734559; DOI=10.1074/jbc.m311194200;
RA Wang L.H., Weng L.X., Dong Y.H., Zhang L.H.;
RT "Specificity and enzyme kinetics of the quorum-quenching N-Acyl homoserine
RT lactone lactonase (AHL-lactonase).";
RL J. Biol. Chem. 279:13645-13651(2004).
CC -!- FUNCTION: Hydrolyzes acyl homoserine lactones with varying lengths of
CC acyl chains, with a slight preference for substrates without 3-oxo
CC substitution at the C3 position. Has only residual activity towards
CC non-acyl lactones, and no activity towards non-cyclic esters.
CC {ECO:0000269|PubMed:14734559}.
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:10716724, ECO:0000269|PubMed:11459062,
CC ECO:0000269|PubMed:14734559};
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 -!- ACTIVITY REGULATION: Completely inhibited by Cu(2+) and Ag(+).
CC Partially inhibited by Cr(2+), Pb(2+) and Fe(2+). Mg(2+), Ca(2+),
CC Mn(2+), Co(2+), Ni(2+), Zn(2+) and Cd(2+) have no effect on activity.
CC The chelating agents EDTA, 2,2'bipyridine and o-phenanthroline have no
CC effect on enzyme activity. {ECO:0000269|PubMed:14734559}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.07 mM for 3-oxo-C4-HSL {ECO:0000269|PubMed:14734559};
CC KM=2.95 mM for 3-oxo-C6-HSL {ECO:0000269|PubMed:14734559};
CC KM=2.28 mM for 3-oxo-C8-HSL {ECO:0000269|PubMed:14734559};
CC KM=1.43 mM for 3-oxo-C10-HSL {ECO:0000269|PubMed:14734559};
CC KM=5.11 mM for C4-HSL {ECO:0000269|PubMed:14734559};
CC KM=3.83 mM for C6-HSL {ECO:0000269|PubMed:14734559};
CC KM=2.61 mM for C8-HSL {ECO:0000269|PubMed:14734559};
CC KM=7.51 mM for 3-HO-C4-HSL {ECO:0000269|PubMed:14734559};
CC pH dependence:
CC Optimum pH is 8.0 with 3-oxo-C8-HSL as substrate. Activity increases
CC with increase in pH from 6.0 to 8.0, and declines slightly at pH 9.0.
CC Little or no activity at pH 5.0 or below.
CC {ECO:0000269|PubMed:14734559};
CC Temperature dependence:
CC Stable below 37 degrees Celsius, activity decreases sharply after
CC incubation for 2 hours at 45 degrees Celsius.
CC {ECO:0000269|PubMed:14734559};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q7B8B9}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC {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; AF196486; AAF62398.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9L8R8; -.
DR SMR; Q9L8R8; -.
DR BioCyc; MetaCyc:MON-14588; -.
DR BRENDA; 3.1.1.81; 691.
DR SABIO-RK; Q9L8R8; -.
DR PHI-base; PHI:2340; -.
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_0000403299"
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 104
FT /note="H->L: Reduces activity on N-beta-oxooctanoyl-L-
FT homoserine lactone by 38.6%; when associated with L-106 and
FT L-108. Reduces activity on N-beta-oxooctanoyl-L-homoserine
FT lactone by 62.1%; when associated with L-106, L-108 and L-
FT 109."
FT /evidence="ECO:0000269|PubMed:10716724"
FT MUTAGEN 104
FT /note="H->S: No effect on activity on N-beta-oxooctanoyl-L-
FT homoserine lactone. Reduces activity on N-beta-oxooctanoyl-
FT L-homoserine lactone by 48.9%; when associated with S-106.
FT Abolishes activity on N-beta-oxooctanoyl-L-homoserine
FT lactone; when associated with S-106 and S-109. Abolishes
FT activity on N-beta-oxooctanoyl-L-homoserine lactone; when
FT associated with S-106, S-108 and S-109."
FT /evidence="ECO:0000269|PubMed:10716724"
FT MUTAGEN 106
FT /note="H->L: Reduces activity on N-beta-oxooctanoyl-L-
FT homoserine lactone by 38.6%; when associated with L-104 and
FT L-108. Reduces activity on N-beta-oxooctanoyl-L-homoserine
FT lactone by 62.1%; when associated with L-104, L-108 and L-
FT 109."
FT /evidence="ECO:0000269|PubMed:10716724,
FT ECO:0000269|PubMed:14734559"
FT MUTAGEN 106
FT /note="H->S: Results in a conformational change. Reduces
FT activity on N-beta-oxooctanoyl-L-homoserine lactone by
FT 38.6%. Reduces activity on acyl homoserine lactone by 47%
FT and decreases enzyme affinity. Reduces activity on N-beta-
FT oxooctanoyl-L-homoserine lactone by 48.9%; when associated
FT with S-104. Abolishes activity on N-beta-oxooctanoyl-L-
FT homoserine lactone; when associated with S-104 and S-109.
FT Abolishes activity on N-beta-oxooctanoyl-L-homoserine
FT lactone; when associated with S-104, S-108 and S-109."
FT /evidence="ECO:0000269|PubMed:10716724,
FT ECO:0000269|PubMed:14734559"
FT MUTAGEN 108
FT /note="D->E: Reduces activity on N-beta-oxooctanoyl-L-
FT homoserine lactone by 9.2%."
FT /evidence="ECO:0000269|PubMed:10716724,
FT ECO:0000269|PubMed:14734559"
FT MUTAGEN 108
FT /note="D->L: Reduces activity on N-beta-oxooctanoyl-L-
FT homoserine lactone by 38.6%; when associated with L-104 and
FT L-106. Reduces activity on N-beta-oxooctanoyl-L-homoserine
FT lactone by 62.1%; when associated with L-104, L-106 and L-
FT 109."
FT /evidence="ECO:0000269|PubMed:10716724,
FT ECO:0000269|PubMed:14734559"
FT MUTAGEN 108
FT /note="D->S: Results in a conformational change. Abolishes
FT activity on N-beta-oxooctanoyl-L-homoserine lactone and
FT acyl homoserine lactone. Abolishes activity on N-beta-
FT oxooctanoyl-L-homoserine lactone; when associated with S-
FT 109. Abolishes activity on N-beta-oxooctanoyl-L-homoserine
FT lactone; when associated with S-104, S-106 and S-109."
FT /evidence="ECO:0000269|PubMed:10716724,
FT ECO:0000269|PubMed:14734559"
FT MUTAGEN 109
FT /note="H->L: Reduces activity on N-beta-oxooctanoyl-L-
FT homoserine lactone by 62.1%; when associated with L-104, L-
FT 106 and L-108."
FT /evidence="ECO:0000269|PubMed:10716724,
FT ECO:0000269|PubMed:14734559"
FT MUTAGEN 109
FT /note="H->S: Results in a conformational change. Abolishes
FT activity on N-beta-oxooctanoyl-L-homoserine lactone and
FT acyl homoserine lactone. Abolishes activity on N-beta-
FT oxooctanoyl-L-homoserine lactone; when associated with S-
FT 108. Abolishes activity on N-beta-oxooctanoyl-L-homoserine
FT lactone; when associated with S-104 and S-106. Abolishes
FT activity on N-beta-oxooctanoyl-L-homoserine lactone; when
FT associated with S-104, S-106 and S-108."
FT /evidence="ECO:0000269|PubMed:10716724,
FT ECO:0000269|PubMed:14734559"
FT MUTAGEN 169
FT /note="H->S: Results in a conformational change. Reduces
FT activity on N-beta-oxooctanoyl-L-homoserine lactone by
FT 38.6%. Reduces activity on acyl homoserine lactone by 47%
FT and decreases enzyme affinity."
FT /evidence="ECO:0000269|PubMed:10716724,
FT ECO:0000269|PubMed:14734559"
SQ SEQUENCE 250 AA; 28037 MW; 6E5D32E1E8818272 CRC64;
MTVKKLYFVP AGRCMLDHSS VNSTLTPGEL LDLPVWCYLL ETEEGPILVD TGMPESAVNN
EGLFNGTFVE GQVLPKMTEE DRIVNILKRV GYEPEDLLYI ISSHLHFDHA GGNGAFINTP
IIVQRAEYEA AQHSEEYLKE CILPNLNYKI IEGDYEVVPG VQLLHTPGHT PGHQSLLIET
EKSGPVLLTI DASYTKENFE NEVPFAGFDS ELALSSIKRL KEVVMKEKPI VFFGHDIEQE
RGCKVFPEYI
