ESAI_PANSE
ID ESAI_PANSE Reviewed; 210 AA.
AC P54656;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Acyl-homoserine-lactone synthase;
DE EC=2.3.1.184;
DE AltName: Full=Autoinducer synthesis protein EsaI;
GN Name=esaI;
OS Pantoea stewartii subsp. stewartii (Erwinia stewartii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=66271;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SS104;
RX PubMed=7665477; DOI=10.1128/jb.177.17.5000-5008.1995;
RA von Bodman S.B., Farrand S.K.;
RT "Capsular polysaccharide biosynthesis and pathogenicity in Erwinia
RT stewartii require induction by an N-acylhomoserine lactone autoinducer.";
RL J. Bacteriol. 177:5000-5008(1995).
CC -!- FUNCTION: Required for the synthesis of OHHL (N-(3-oxohexanoyl)-L-
CC homoserine lactone), an autoinducer molecule which binds to EsaR. OHHL
CC is necessary for biosynthesis of EPS virulence factor (extracellular
CC heteropolysaccharide) which plays a role in the development of
CC Stewart's wilt on sweet corn.
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; L32183; AAA82096.1; -; Genomic_DNA.
DR PIR; A57337; A57337.
DR RefSeq; WP_006119202.1; NZ_VZPF01000009.1.
DR PDB; 1K4J; X-ray; 2.50 A; A=1-210.
DR PDB; 1KZF; X-ray; 1.80 A; A=1-210.
DR PDBsum; 1K4J; -.
DR PDBsum; 1KZF; -.
DR AlphaFoldDB; P54656; -.
DR SMR; P54656; -.
DR GeneID; 61251106; -.
DR EvolutionaryTrace; P54656; -.
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; 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;
KW S-adenosyl-L-methionine; Transferase; Virulence.
FT CHAIN 1..210
FT /note="Acyl-homoserine-lactone synthase"
FT /id="PRO_0000210884"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:1KZF"
FT HELIX 9..14
FT /evidence="ECO:0007829|PDB:1KZF"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:1KZF"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:1KZF"
FT STRAND 62..71
FT /evidence="ECO:0007829|PDB:1KZF"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:1KZF"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:1KZF"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:1KZF"
FT HELIX 105..112
FT /evidence="ECO:0007829|PDB:1KZF"
FT HELIX 118..132
FT /evidence="ECO:0007829|PDB:1KZF"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:1KZF"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:1KZF"
FT STRAND 158..168
FT /evidence="ECO:0007829|PDB:1KZF"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:1KZF"
FT HELIX 180..194
FT /evidence="ECO:0007829|PDB:1KZF"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:1KZF"
FT STRAND 202..208
FT /evidence="ECO:0007829|PDB:1KZF"
SQ SEQUENCE 210 AA; 23844 MW; 7FCCF1F3709D50F5 CRC64;
MLELFDVSYE ELQTTRSEEL YKLRKKTFSD RLGWEVICSQ GMESDEFDGP GTRYILGICE
GQLVCSVRFT SLDRPNMITH TFQHCFSDVT LPAYGTESSR FFVDKARARA LLGEHYPISQ
VLFLAMVNWA QNNAYGNIYT IVSRAMLKIL TRSGWQIKVI KEAFLTEKER IYLLTLPAGQ
DDKQQLGGDV VSRTGCPPVA VTTWPLTLPV