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