AHLLA_BACTK
ID AHLLA_BACTK Reviewed; 250 AA.
AC P0CJ63; Q7B8B9; Q8RPW7; Q8RPW8;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=N-acyl homoserine lactonase AiiA;
DE Short=AHL-lactonase AiiA;
DE EC=3.1.1.81;
GN Name=aiiA;
OS Bacillus thuringiensis subsp. kurstaki.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=29339;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B1, and B2 / BGSC 4D1;
RX PubMed=11916693; DOI=10.1128/aem.68.4.1754-1759.2002;
RA Dong Y.H., Gusti A.R., Zhang Q., Xu J.L., Zhang L.H.;
RT "Identification of quorum-quenching N-acyl homoserine lactonases from
RT Bacillus species.";
RL Appl. Environ. Microbiol. 68:1754-1759(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=HD-263;
RX PubMed=12147491; DOI=10.1128/aem.68.8.3919-3924.2002;
RA Lee S.J., Park S.Y., Lee J.J., Yum D.Y., Koo B.T., Lee J.K.;
RT "Genes encoding the N-acyl homoserine lactone-degrading enzyme are
RT widespread in many subspecies of Bacillus thuringiensis.";
RL Appl. Environ. Microbiol. 68:3919-3924(2002).
RN [3]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASP-108; TYR-194; ALA-206
RP AND GLY-207.
RX PubMed=18627130; DOI=10.1021/bi8003704;
RA Momb J., Wang C., Liu D., Thomas P.W., Petsko G.A., Guo H., Ringe D.,
RA Fast W.;
RT "Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus
RT thuringiensis. 2. Substrate modeling and active site mutations.";
RL Biochemistry 47:7715-7725(2008).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), COFACTOR, SUBUNIT, AND ZINC-BINDING.
RX PubMed=16087890; DOI=10.1073/pnas.0505255102;
RA Liu D., Lepore B.W., Petsko G.A., Thomas P.W., Stone E.M., Fast W.,
RA Ringe D.;
RT "Three-dimensional structure of the quorum-quenching N-acyl homoserine
RT lactone hydrolase from Bacillus thuringiensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11882-11887(2005).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), X-RAY CRYSTALLOGRAPHY (1.7
RP ANGSTROMS) IN COMPLEX WITH L-HOMOSERINE LACTONE, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, ZINC-BINDING, AND MUTAGENESIS OF HIS-104; HIS-106;
RP ASP-108; HIS-109; ASP-191; TYR-194 AND HIS-235.
RX PubMed=16314577; DOI=10.1073/pnas.0504996102;
RA Kim M.H., Choi W.C., Kang H.O., Lee J.S., Kang B.S., Kim K.J.,
RA Derewenda Z.S., Oh T.K., Lee C.H., Lee J.K.;
RT "The molecular structure and catalytic mechanism of a quorum-quenching N-
RT acyl-L-homoserine lactone hydrolase.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:17606-17611(2005).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (0.95 ANGSTROMS) IN COMPLEX WITH PRODUCT.
RX PubMed=18627129; DOI=10.1021/bi800368y;
RA Liu D., Momb J., Thomas P.W., Moulin A., Petsko G.A., Fast W., Ringe D.;
RT "Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus
RT thuringiensis. 1. Product-bound structures.";
RL Biochemistry 47:7706-7714(2008).
CC -!- FUNCTION: Catalyzes hydrolysis of N-hexanoyl-(S)-homoserine lactone,
CC but not the R-enantiomer. Hydrolyzes short- and long-chain N-acyl
CC homoserine lactones with or without 3-oxo substitution at C3, has
CC maximum activity on C10-AHL. {ECO:0000269|PubMed:16314577}.
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:16314577};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16087890, ECO:0000269|PubMed:16314577};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:16087890,
CC ECO:0000269|PubMed:16314577};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=303 mM for GBL (with cobalt as cofactor)
CC {ECO:0000269|PubMed:18627130};
CC KM=0.8 mM for C5-HSL (with cobalt as cofactor)
CC {ECO:0000269|PubMed:18627130};
CC KM=0.15 mM for C10-HSL (with cobalt as cofactor)
CC {ECO:0000269|PubMed:18627130};
CC KM=3.8 mM for BOC-HSL (with cobalt as cofactor)
CC {ECO:0000269|PubMed:18627130};
CC KM=0.48 mM for CBZ-HSL (with cobalt as cofactor)
CC {ECO:0000269|PubMed:18627130};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16087890,
CC ECO:0000269|PubMed:16314577, ECO:0000269|PubMed:18627129}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC {ECO:0000305}.
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DR EMBL; AF350928; AAL98717.1; -; Genomic_DNA.
DR EMBL; AF350929; AAL98718.1; -; Genomic_DNA.
DR EMBL; AF478059; AAM92140.1; -; Genomic_DNA.
DR RefSeq; WP_000216581.1; NZ_PHSM01000001.1.
DR PDB; 2A7M; X-ray; 1.60 A; A=1-250.
DR PDB; 2BR6; X-ray; 1.70 A; A=1-250.
DR PDB; 2BTN; X-ray; 2.00 A; A=1-250.
DR PDB; 3DHA; X-ray; 0.95 A; A=1-250.
DR PDB; 3DHB; X-ray; 1.40 A; A=1-250.
DR PDB; 3DHC; X-ray; 1.30 A; A=1-250.
DR PDB; 5EH9; X-ray; 1.29 A; A=2-250.
DR PDB; 7L5F; X-ray; 1.51 A; A=1-250.
DR PDBsum; 2A7M; -.
DR PDBsum; 2BR6; -.
DR PDBsum; 2BTN; -.
DR PDBsum; 3DHA; -.
DR PDBsum; 3DHB; -.
DR PDBsum; 3DHC; -.
DR PDBsum; 5EH9; -.
DR PDBsum; 7L5F; -.
DR AlphaFoldDB; P0CJ63; -.
DR SMR; P0CJ63; -.
DR BRENDA; 3.1.1.25; 711.
DR BRENDA; 3.1.1.81; 711.
DR EvolutionaryTrace; P0CJ63; -.
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 3D-structure; Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..250
FT /note="N-acyl homoserine lactonase AiiA"
FT /id="PRO_0000399991"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT MUTAGEN 104
FT /note="H->A: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:16314577"
FT MUTAGEN 106
FT /note="H->A: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:16314577"
FT MUTAGEN 108
FT /note="D->A: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:16314577,
FT ECO:0000269|PubMed:18627130"
FT MUTAGEN 108
FT /note="D->N: Slow substrate turnover."
FT /evidence="ECO:0000269|PubMed:16314577,
FT ECO:0000269|PubMed:18627130"
FT MUTAGEN 109
FT /note="H->A: Reduces activity by 85%."
FT /evidence="ECO:0000269|PubMed:16314577"
FT MUTAGEN 169
FT /note="H->A: Abolishes activity."
FT MUTAGEN 191
FT /note="D->A: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:16314577"
FT MUTAGEN 191
FT /note="D->L: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:16314577"
FT MUTAGEN 194
FT /note="Y->F: Reduces activity by 70%. Slow substrate
FT turnover."
FT /evidence="ECO:0000269|PubMed:16314577,
FT ECO:0000269|PubMed:18627130"
FT MUTAGEN 206
FT /note="A->W: Small decrease in KM value for hydrolysis of
FT GBL, C5-HSL and C10-HSL."
FT /evidence="ECO:0000269|PubMed:18627130"
FT MUTAGEN 207
FT /note="G->D: Small decrease in KM value for hydrolysis of
FT GBL and C10-HSL. Increase in KM value for hydrolysis of C5-
FT HSL."
FT /evidence="ECO:0000269|PubMed:18627130"
FT MUTAGEN 207
FT /note="G->W: Small decrease in KM value for hydrolysis of
FT GBL and C5-HSL. Larger decrease in KM value for hydrolysis
FT of C10-HSL."
FT /evidence="ECO:0000269|PubMed:18627130"
FT MUTAGEN 235
FT /note="H->A: Reduces activity by 85%."
FT /evidence="ECO:0000269|PubMed:16314577"
FT CONFLICT 189
FT /note="T -> M (in Ref. 1; AAL98717)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="I -> T (in Ref. 1; AAL98717)"
FT /evidence="ECO:0000305"
FT STRAND 3..17
FT /evidence="ECO:0007829|PDB:3DHA"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:3DHA"
FT STRAND 30..42
FT /evidence="ECO:0007829|PDB:3DHA"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:3DHA"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:3DHA"
FT TURN 61..66
FT /evidence="ECO:0007829|PDB:3DHA"
FT TURN 68..72
FT /evidence="ECO:0007829|PDB:3DHA"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:3DHA"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:3DHA"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:3DHA"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:3DHA"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:3DHA"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:3DHA"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:3DHA"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:3DHA"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:3DHA"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:3DHA"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:3DHA"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:3DHA"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:3DHA"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:3DHA"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:3DHA"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:3DHA"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:3DHA"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:3DHA"
FT HELIX 196..200
FT /evidence="ECO:0007829|PDB:3DHA"
FT HELIX 210..227
FT /evidence="ECO:0007829|PDB:3DHA"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:3DHA"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:3DHA"
SQ SEQUENCE 250 AA; 28220 MW; CEBC2FE957707C2E CRC64;
MTVKKLYFIP AGRCMLDHSS VNSALTPGKL LNLPVWCYLL ETEEGPILVD TGMPESAVNN
EGLFNGTFVE GQILPKMTEE DRIVNILKRV GYEPDDLLYI ISSHLHFDHA GGNGAFTNTP
IIVQRTEYEA ALHREEYMKE CILPHLNYKI IEGDYEVVPG VQLLYTPGHS PGHQSLFIET
EQSGSVLLTI DASYTKENFE DEVPFAGFDP ELALSSIKRL KEVVKKEKPI IFFGHDIEQE
KSCRVFPEYI
