ID   ANOI_ACINO              Reviewed;         183 AA.
AC   A0A0A7XNA3;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   04-MAR-2015, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=Acyl-homoserine-lactone synthase {ECO:0000305};
DE            EC=2.3.1.184 {ECO:0000250|UniProtKB:B0FLN1};
DE   AltName: Full=Autoinducer synthesis protein AnoI {ECO:0000305};
GN   Name=anoI {ECO:0000303|PubMed:25975610};
GN   ORFNames=RR32_17480 {ECO:0000312|EMBL:AJB49806.1};
OS   Acinetobacter nosocomialis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=106654;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6411;
RA   McCorrison J., Sanka R., Adams M., Brinkac L., Sutton G., Bonomo R.,
RA   Rojas L.;
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 17903;
RX   PubMed=25975610; DOI=10.4014/jmb.1504.04069;
RA   Oh M.H., Choi C.H.;
RT   "Role of LuxIR homologue AnoIR in Acinetobacter nosocomialis and the effect
RT   of virstatin on the expression of anoR gene.";
RL   J. Microbiol. Biotechnol. 25:1390-1400(2015).
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). Probably part of a quorum-sensing system with AnoR.
CC       {ECO:0000269|PubMed:25975610}.
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:0000250|UniProtKB:B0FLN1};
CC   -!- INDUCTION: Positively regulated by AnoR. {ECO:0000269|PubMed:25975610}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant does not produce OH-dDHL.
CC       {ECO:0000269|PubMed:25975610}.
CC   -!- SIMILARITY: Belongs to the autoinducer synthase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00533}.
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DR   EMBL; CP010368; AJB49806.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A7XNA3; -.
DR   SMR; A0A0A7XNA3; -.
DR   STRING; 106654.B7L44_20130; -.
DR   KEGG; ano:RR32_17480; -.
DR   PATRIC; fig|106654.21.peg.3488; -.
DR   eggNOG; COG3916; Bacteria.
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   2: Evidence at transcript level;
KW   Autoinducer synthesis; Quorum sensing; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..183
FT                   /note="Acyl-homoserine-lactone synthase"
FT                   /id="PRO_0000438127"
SQ   SEQUENCE   183 AA;  20270 MW;  C1D2513C19B5CDB1 CRC64;
     MNIIAGFQNN FSEGLYSKFK SYRYKVFVEH LGWELNCPHN EELDQFDKVD TAYVVAQDRD
     SNIIGCARLL PTTQPYLLGE IFPQLLNGIP LPCSPEIWEL SRFSAVDFSN PPTTASQAVS
     SPVSIAILQE AINFARAQGA KQLITTSPLG VERLLRAAGF RAHRAGPPMT IDGYSMFACL
     IDV