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CARI_PECCC
ID   CARI_PECCC              Reviewed;         216 AA.
AC   P33880;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Acyl-homoserine-lactone synthase;
DE            EC=2.3.1.184;
DE   AltName: Full=Autoinducer synthesis protein CarI;
GN   Name=carI; Synonyms=hslI;
OS   Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp.
OS   carotovora).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 39048 / GS101 / SC 12;
RX   PubMed=7968529; DOI=10.1111/j.1365-2958.1993.tb00923.x;
RA   Swift S., Winson M.K., Chan P.F., Bainton N.J., Birdsall M., Reeves P.J.,
RA   Rees C.E.D., Chhabra S.R., Hill P.J., Throup J.P., Bycroft B.W.,
RA   Salmond G.P.C., Williams P., Stewart G.S.A.B.;
RT   "A novel strategy for the isolation of luxI homologues: evidence for the
RT   widespread distribution of a LuxR:LuxI superfamily in enteric bacteria.";
RL   Mol. Microbiol. 10:511-520(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=71;
RA   Chatterjee A., Cui Y., Liu Y., Dumenyo C.K., Chatterjee A.K.;
RL   Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for the synthesis of OHHL (N-(3-oxohexanoyl)-L-
CC       homoserine lactone), an autoinducer molecule which binds to CarR and
CC       thus acts in the control of the biosynthesis of carbapenem antibiotics.
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; X74299; CAA52352.1; -; Genomic_DNA.
DR   EMBL; L40174; AAA62483.1; -; Genomic_DNA.
DR   PIR; S35947; S35947.
DR   AlphaFoldDB; P33880; -.
DR   SMR; P33880; -.
DR   GO; GO:0061579; F:N-acyl homoserine lactone synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
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   Antibiotic biosynthesis; Autoinducer synthesis; Quorum sensing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..216
FT                   /note="Acyl-homoserine-lactone synthase"
FT                   /id="PRO_0000210881"
FT   CONFLICT        18
FT                   /note="G -> E (in Ref. 2; AAA62483)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        132
FT                   /note="K -> R (in Ref. 2; AAA62483)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        208..209
FT                   /note="RV -> KG (in Ref. 2; AAA62483)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   216 AA;  25067 MW;  F6C6F4148E9B5D57 CRC64;
     MLEIFDVNHT LLSETKSGEL FTLRKETFKD RLNWAVQCTD GMEFDQYDNN NTTYLFGIKD
     NTVICSLRFI ETKYPNMITG TFFPYFKEIN IPEGNYLESS RFFVDKSRAK DILGNEYPIS
     SMLFLSMINY SKDKGYDGIY TIVSHPMLTI LKRSGWGIRV VEQGLSEKEE RVYLVFLPVD
     DENQEALARR INRSGTFMSN ELKQWPLRVP AAIAQA
 
 
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