ID   AHLLB_AGRRK             Reviewed;         276 AA.
AC   B9JPK6;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=N-acyl homoserine lactonase AiiB {ECO:0000250|UniProtKB:A9CKY2};
DE            Short=AHL-lactonase AiiB {ECO:0000250|UniProtKB:A9CKY2};
DE            EC=3.1.1.81;
GN   Name=aiiB {ECO:0000250|UniProtKB:A9CKY2}; OrderedLocusNames=Arad_14225;
OS   Agrobacterium radiobacter (strain K84 / ATCC BAA-868).
OG   Plasmid pAtK84b {ECO:0000312|EMBL:ACM31075.1}.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=311403;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K84 / ATCC BAA-868;
RX   PubMed=19251847; DOI=10.1128/jb.01779-08;
RA   Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K.,
RA   Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., Otten L.,
RA   Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., Du Z., Ewing A.,
RA   Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., Miller N.M.,
RA   Norton S., Chen Q., Phoolcharoen W., Ohlin V., Ondrusek D., Pride N.,
RA   Stricklin S.L., Sun J., Wheeler C., Wilson L., Zhu H., Wood D.W.;
RT   "Genome sequences of three Agrobacterium biovars help elucidate the
RT   evolution of multichromosome genomes in bacteria.";
RL   J. Bacteriol. 191:2501-2511(2009).
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:0000250|UniProtKB:A9CKY2};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:A9CKY2};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:A9CKY2};
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP000630; ACM31075.1; -; Genomic_DNA.
DR   RefSeq; WP_012655005.1; NC_011990.1.
DR   AlphaFoldDB; B9JPK6; -.
DR   SMR; B9JPK6; -.
DR   EnsemblBacteria; ACM31075; ACM31075; Arad_14225.
DR   KEGG; ara:Arad_14225; -.
DR   HOGENOM; CLU_030571_3_2_5; -.
DR   OMA; GMMTYQH; -.
DR   OrthoDB; 1815576at2; -.
DR   Proteomes; UP000001600; Plasmid pAtK84b.
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   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Plasmid; Reference proteome; Zinc.
FT   CHAIN           1..276
FT                   /note="N-acyl homoserine lactonase AiiB"
FT                   /id="PRO_0000403992"
FT   BINDING         111
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:A9CKY2"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:A9CKY2"
FT   BINDING         116
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:A9CKY2"
FT   BINDING         191
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:A9CKY2"
FT   BINDING         213
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:A9CKY2"
FT   BINDING         213
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:A9CKY2"
FT   BINDING         259
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:A9CKY2"
SQ   SEQUENCE   276 AA;  30617 MW;  04C8CE21B17CCE23 CRC64;
     MGNKLFVLDL GEIRVDENFI IANSTFVTPQ KPTVSSRLID IPVSAYLIQC TNATILYDTG
     CHPECMGTNG RWPAQSQLNA PYIGASECNL PERLRQLDLS PDDISTVVLS HLHNDHAGCV
     EFFGKSRLIA HEDEFATAVR YFATGDHSSP YIVKDIEAWL ATPRNWDLVG RDERERELAP
     GVNLLNFGTG HASGMLGLAV RLEKQPGFLL VSDACYTATN YGPPARRAGV LHDTIGYDRT
     VSHIRQYAES RSLTVLFGHD REQFASLIKS TDGFYE