ID   ABAI_ACIBA              Reviewed;         184 AA.
AC   B0FLN1;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Acyl-homoserine-lactone synthase {ECO:0000305};
DE            EC=2.3.1.184 {ECO:0000269|PubMed:18281398};
DE   AltName: Full=Autoinducer synthesis protein AbaI {ECO:0000305};
GN   Name=abaI {ECO:0000303|PubMed:18281398};
OS   Acinetobacter baumannii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=470;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, INDUCTION,
RP   AND DISRUPTION PHENOTYPE.
RC   STRAIN=M2;
RX   PubMed=18281398; DOI=10.1128/jb.01929-07;
RA   Niu C., Clemmer K.M., Bonomo R.A., Rather P.N.;
RT   "Isolation and characterization of an autoinducer synthase from
RT   Acinetobacter baumannii.";
RL   J. Bacteriol. 190:3386-3392(2008).
CC   -!- FUNCTION: Involved in the synthesis of the acyl-homoserine lactone
CC       (AHL) signal N-(3-hydroxydodecanoyl)-L-HSL (3-hydroxy-C(12)-HSL or OH-
CC       dDHL). Required for normal biofilm development.
CC       {ECO:0000269|PubMed:18281398}.
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; Evidence={ECO:0000269|PubMed:18281398};
CC   -!- INDUCTION: Expression is activated by AHL signals in a positive-
CC       feedback loop. {ECO:0000269|PubMed:18281398}.
CC   -!- DISRUPTION PHENOTYPE: Mutant fails to produce any detectable AHL
CC       signals and is impaired in biofilm development.
CC       {ECO:0000269|PubMed:18281398}.
CC   -!- SIMILARITY: Belongs to the autoinducer synthase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00533}.
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DR   EMBL; EU334497; ABY50954.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0FLN1; -.
DR   SMR; B0FLN1; -.
DR   STRING; 470.IX87_15130; -.
DR   eggNOG; COG3916; Bacteria.
DR   BRENDA; 2.3.1.184; 98.
DR   PHI-base; PHI:8774; -.
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; 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; PS51187; AUTOINDUCER_SYNTH_2; 1.
PE   1: Evidence at protein level;
KW   Autoinducer synthesis; Quorum sensing; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..184
FT                   /note="Acyl-homoserine-lactone synthase"
FT                   /id="PRO_0000438126"
SQ   SEQUENCE   184 AA;  20594 MW;  821A9954CBFF8BE8 CRC64;
     MNIIAGFQNN FSEGLYTKFK SYRYRVFVEY LGWELNCPNN EETRIQFDKV DTAYVVAQDR
     ESNIIGCARL LPTTQPYLLG EIFPQLLNGM PIPCSPEIWE LSRFSAVDFS KPPSSSSQAV
     SSPISIAILQ EAINFAREQG AKQLITTSPL GVERLLRAAG FRAHRAGPPM MIDGYSMFAC
     LIDV