LASI_PSEAE
ID LASI_PSEAE Reviewed; 201 AA.
AC P33883;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Acyl-homoserine-lactone synthase;
DE EC=2.3.1.184;
DE AltName: Full=Autoinducer synthesis protein LasI;
GN Name=lasI; OrderedLocusNames=PA1432;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=8493556; DOI=10.1126/science.8493556;
RA Passador L., Cook J.M., Gambello M.J., Rust L., Iglewski B.H.;
RT "Expression of Pseudomonas aeruginosa virulence genes requires cell-to-cell
RT communication.";
RL Science 260:1127-1130(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP STRUCTURE OF INDUCER.
RX PubMed=8278364; DOI=10.1073/pnas.91.1.197;
RA Pearson J.P., Gray K., Passador L., Tucker K.D., Eberhard A.,
RA Iglewski B.H., Greenberg E.P.;
RT "Structure of the autoinducer required for expression of Pseudomonas
RT aeruginosa virulence genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:197-201(1994).
CC -!- FUNCTION: Required for the synthesis of PAI consisting of 3-oxo-N-
CC (tetrahydro-2-oxo-3-furanyl)-dodecanamide also known as N-(3-
CC oxododecanoyl)homoserine lactone, an autoinducer molecule which binds
CC to LasR and thus acts in elastase biosynthesis regulation.
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; L04681; AAA25875.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04821.1; -; Genomic_DNA.
DR PIR; G83467; G83467.
DR RefSeq; NP_250123.1; NC_002516.2.
DR RefSeq; WP_003083017.1; NZ_QZGE01000005.1.
DR PDB; 1RO5; X-ray; 2.30 A; A=1-201.
DR PDBsum; 1RO5; -.
DR AlphaFoldDB; P33883; -.
DR SMR; P33883; -.
DR STRING; 287.DR97_591; -.
DR ChEMBL; CHEMBL1795157; -.
DR PaxDb; P33883; -.
DR PRIDE; P33883; -.
DR DNASU; 881777; -.
DR EnsemblBacteria; AAG04821; AAG04821; PA1432.
DR GeneID; 881777; -.
DR KEGG; pae:PA1432; -.
DR PATRIC; fig|208964.12.peg.1481; -.
DR PseudoCAP; PA1432; -.
DR HOGENOM; CLU_085711_4_0_6; -.
DR OMA; YMLKDTF; -.
DR PhylomeDB; P33883; -.
DR BioCyc; MetaCyc:MON-14567; -.
DR BioCyc; PAER208964:G1FZ6-1458-MON; -.
DR BRENDA; 2.3.1.184; 5087.
DR EvolutionaryTrace; P33883; -.
DR PHI-base; PHI:6997; -.
DR Proteomes; UP000002438; 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 GO; GO:0007165; P:signal transduction; IDA:PseudoCAP.
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 1: Evidence at protein level;
KW 3D-structure; Autoinducer synthesis; Quorum sensing; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..201
FT /note="Acyl-homoserine-lactone synthase"
FT /id="PRO_0000210887"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1RO5"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:1RO5"
FT HELIX 13..27
FT /evidence="ECO:0007829|PDB:1RO5"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:1RO5"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:1RO5"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:1RO5"
FT STRAND 64..73
FT /evidence="ECO:0007829|PDB:1RO5"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:1RO5"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:1RO5"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:1RO5"
FT HELIX 118..133
FT /evidence="ECO:0007829|PDB:1RO5"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:1RO5"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:1RO5"
FT HELIX 146..154
FT /evidence="ECO:0007829|PDB:1RO5"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:1RO5"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:1RO5"
FT STRAND 171..179
FT /evidence="ECO:0007829|PDB:1RO5"
FT HELIX 182..189
FT /evidence="ECO:0007829|PDB:1RO5"
SQ SEQUENCE 201 AA; 22691 MW; DBE8582AF42B9AA6 CRC64;
MIVQIGRREE FDKKLLGEMH KLRAQVFKER KGWDVSVIDE MEIDGYDALS PYYMLIQEDT
PEAQVFGCWR ILDTTGPYML KNTFPELLHG KEAPCSPHIW ELSRFAINSG QKGSLGFSDC
TLEAMRALAR YSLQNDIQTL VTVTTVGVEK MMIRAGLDVS RFGPHLKIGI ERAVALRIEL
NAKTQIALYG GVLVEQRLAV S
