ID   AHLL_MICTS              Reviewed;         251 AA.
AC   C6L862; E8N9C9;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 2.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=N-acyl homoserine lactonase {ECO:0000303|PubMed:20173075};
DE            Short=AHL-lactonase {ECO:0000303|PubMed:20173075};
DE            EC=3.1.1.81;
GN   Name=aiiM; OrderedLocusNames=MTES_2811;
OS   Microbacterium testaceum (strain StLB037).
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Microbacterium.
OX   NCBI_TaxID=979556;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=StLB037;
RX   PubMed=20173075; DOI=10.1128/aem.02738-09;
RA   Wang W., Morohoshi T., Ikenoya M., Someya N., Ikeda T.;
RT   "AiiM, a novel class of N-acylhomoserine lactonase from the leaf-associated
RT   bacterium Microbacterium testaceum.";
RL   Appl. Environ. Microbiol. 76:2524-2530(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=StLB037;
RX   PubMed=21357489; DOI=10.1128/jb.00180-11;
RA   Morohoshi T., Wang W.Z., Someya N., Ikeda T.;
RT   "Genome sequence of Microbacterium testaceum StLB037, an N-acylhomoserine
RT   lactone-degrading bacterium isolated from potato leaves.";
RL   J. Bacteriol. 193:2072-2073(2011).
CC   -!- FUNCTION: Hydrolyzes short- and long-chain N-acyl homoserine lactones
CC       with or without 3-oxo substitution at C3. Has slight activity towards
CC       L-homoserine lactone, and no activity towards gamma-butyrolactone.
CC       {ECO:0000269|PubMed:20173075}.
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:20173075};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.0. Little or no activity below pH 4.2.
CC         {ECO:0000269|PubMed:20173075};
CC       Temperature dependence:
CC         Retains over 80% of maximum activity at 15 to 60 degrees Celsius.
CC         Activity is greatly reduced over 70 degrees Celsius.
CC         {ECO:0000269|PubMed:20173075};
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DR   EMBL; AB513359; BAH97082.2; -; Genomic_DNA.
DR   EMBL; AP012052; BAJ75775.1; -; Genomic_DNA.
DR   RefSeq; WP_013585900.1; NC_015125.1.
DR   AlphaFoldDB; C6L862; -.
DR   SMR; C6L862; -.
DR   STRING; 979556.MTES_2811; -.
DR   EnsemblBacteria; BAJ75775; BAJ75775; MTES_2811.
DR   KEGG; mts:MTES_2811; -.
DR   eggNOG; COG2267; Bacteria.
DR   HOGENOM; CLU_020336_31_1_11; -.
DR   OMA; YWEEILR; -.
DR   OrthoDB; 1119700at2; -.
DR   BRENDA; 3.1.1.81; 12710.
DR   Proteomes; UP000008975; Chromosome.
DR   GO; GO:0102007; F:acyl-L-homoserine-lactone lactonohydrolase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   Pfam; PF12697; Abhydrolase_6; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..251
FT                   /note="N-acyl homoserine lactonase"
FT                   /id="PRO_0000403303"
SQ   SEQUENCE   251 AA;  27261 MW;  E410BD282A71BC6D CRC64;
     MILAHDVSGS GPLLVLLHGI TEDRRSWDPV DFTDGFTVVR VDLRGHGASA AEEPYDIPTL
     ATDVHDTLAQ LAENDVIPGE LPVIVGHSMG GIVATAYGAL FPARAIVNVD QPLQLAGMQG
     QVQQAEGMLR GADFPLFIHG MFAQMAGGLD AEELARVNGI RSPRQDVVLG MWRPLLEDSP
     EELAALVSGL TRIPEDVPYL VITGLDAGPE YAAWLQREIP QAVQEVWQPP THYPHLVDPA
     RFVERVEAFV R