ID   EXPI_PECPM              Reviewed;         217 AA.
AC   P33882; K4FPM6;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Acyl-homoserine-lactone synthase;
DE            EC=2.3.1.184;
DE   AltName: Full=Autoinducer synthesis protein ExpI;
GN   Name=expI; OrderedLocusNames=W5S_4607;
OS   Pectobacterium parmentieri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=1905730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SCC3193;
RX   PubMed=8508772; DOI=10.1002/j.1460-2075.1993.tb05901.x;
RA   Pirhonen M., Flego D., Heikinheimo R., Palva E.T.;
RT   "A small diffusible signal molecule is responsible for the global control
RT   of virulence and exoenzyme production in the plant pathogen Erwinia
RT   carotovora.";
RL   EMBO J. 12:2467-2476(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SCC3193;
RA   Heikinheimo R., Mae A., Flego D., Pirhonen M., Koiv V., Palva E.T.;
RL   Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCC3193;
RX   PubMed=23045508; DOI=10.1128/jb.00681-12;
RA   Koskinen J.P., Laine P., Niemi O., Nykyri J., Harjunpaa H., Auvinen P.,
RA   Paulin L., Pirhonen M., Palva T., Holm L.;
RT   "Genome sequence of Pectobacterium sp. strain SCC3193.";
RL   J. Bacteriol. 194:6004-6004(2012).
CC   -!- FUNCTION: Required for the synthesis of OHHL (N-(3-oxohexanoyl)-L-
CC       homoserine lactone), an autoinducer molecule which binds to ExpR and
CC       thus acts in virulence (soft rot disease) through the activation of
CC       genes for plant tissue macerating enzymes.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-[ACP] + S-adenosyl-L-methionine = an N-acyl-L-
CC         homoserine lactone + H(+) + holo-[ACP] + S-methyl-5'-thioadenosine;
CC         Xref=Rhea:RHEA:10096, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:14125,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:55474,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:64479, ChEBI:CHEBI:138651;
CC         EC=2.3.1.184;
CC   -!- SIMILARITY: Belongs to the autoinducer synthase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00533}.
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DR   EMBL; X72891; CAA51409.1; -; Genomic_DNA.
DR   EMBL; X80475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP003415; AFI92653.1; -; Genomic_DNA.
DR   PIR; S35324; S35324.
DR   RefSeq; WP_014702025.1; NZ_QESW01000003.1.
DR   AlphaFoldDB; P33882; -.
DR   SMR; P33882; -.
DR   STRING; 1905730.W5S_4607; -.
DR   EnsemblBacteria; AFI92653; AFI92653; W5S_4607.
DR   KEGG; pec:W5S_4607; -.
DR   PATRIC; fig|1166016.3.peg.4669; -.
DR   eggNOG; COG3916; Bacteria.
DR   HOGENOM; CLU_085711_4_1_6; -.
DR   OMA; NCINGME; -.
DR   OrthoDB; 1725271at2; -.
DR   Proteomes; UP000008044; Chromosome.
DR   GO; GO:0061579; F:N-acyl homoserine lactone synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009372; P:quorum sensing; IEA:UniProtKB-KW.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR018311; Autoind_synth_CS.
DR   InterPro; IPR001690; Autoind_synthase.
DR   PANTHER; PTHR39322; PTHR39322; 1.
DR   Pfam; PF00765; Autoind_synth; 1.
DR   PRINTS; PR01549; AUTOINDCRSYN.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS00949; AUTOINDUCER_SYNTH_1; 1.
DR   PROSITE; PS51187; AUTOINDUCER_SYNTH_2; 1.
PE   3: Inferred from homology;
KW   Autoinducer synthesis; Quorum sensing; S-adenosyl-L-methionine;
KW   Transferase; Virulence.
FT   CHAIN           1..217
FT                   /note="Acyl-homoserine-lactone synthase"
FT                   /id="PRO_0000210885"
SQ   SEQUENCE   217 AA;  25321 MW;  12F0979D20FDFE5D CRC64;
     MLEIFDVSYT LLSEKKSEEL FTLRKETFKD RLNWAVKCIN GMEFDQYDDD NATYLFGVEG
     DQVICSSRLI ETKYPNMITG TFFPYFEKID IPEGKYIESS RFFVDKARSK TILGNSYPVS
     TMFFLATVNY SKSKGYDGVY TIVSHPMLTI LKRSGWKISI VEQGMSEKHE RVYLLFLPVD
     NESQDVLVRR INHNQEFVES KLREWPLSFE PMTEPVG