(data stored in ACNUC9543 zone)

SWISSPROT: A0A0E1NPQ8_YERPA

ID   A0A0E1NPQ8_YERPA        Unreviewed;       216 AA.
AC   A0A0E1NPQ8;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   16-JAN-2019, entry version 19.
DE   RecName: Full=Acyl-homoserine-lactone synthase {ECO:0000256|RuleBase:RU361135};
DE            EC=2.3.1.184 {ECO:0000256|RuleBase:RU361135};
DE   AltName: Full=Autoinducer synthesis protein {ECO:0000256|RuleBase:RU361135};
GN   OrderedLocusNames=YPA_0280 {ECO:0000313|EMBL:ABG12249.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12249.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12249.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12249.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-[ACP] + S-adenosyl-L-methionine = an N-acyl-
CC         L-homoserine lactone + H(+) + holo-[ACP] + S-methyl-5'-
CC         thioadenosine; Xref=Rhea:RHEA:10096, Rhea:RHEA-COMP:9685,
CC         Rhea:RHEA-COMP:14125, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509,
CC         ChEBI:CHEBI:55474, ChEBI:CHEBI:59789, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:138651; EC=2.3.1.184;
CC         Evidence={ECO:0000256|RuleBase:RU361135};
CC   -!- SIMILARITY: Belongs to the autoinducer synthase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU00533,
CC       ECO:0000256|RuleBase:RU361135}.
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DR   EMBL; CP000308; ABG12249.1; -; Genomic_DNA.
DR   RefSeq; WP_002215903.1; NZ_CP009906.1.
DR   EnsemblBacteria; ABG12249; ABG12249; YPA_0280.
DR   EnsemblBacteria; AJJ78222; AJJ78222; CH58_3125.
DR   KEGG; ypa:YPA_0280; -.
DR   PATRIC; fig|360102.15.peg.3280; -.
DR   KO; K22956; -.
DR   OMA; THIYTIV; -.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0061579; F:N-acyl homoserine lactone synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009372; P:quorum sensing; IEA:UniProtKB-UniRule.
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;
DR   PRODOM; A0A0E1NPQ8.
DR   SWISS-2DPAGE; A0A0E1NPQ8.
KW   Autoinducer synthesis {ECO:0000256|PROSITE-ProRule:PRU00533,
KW   ECO:0000256|RuleBase:RU361135};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Quorum sensing {ECO:0000256|PROSITE-ProRule:PRU00533,
KW   ECO:0000256|RuleBase:RU361135};
KW   S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU361135};
KW   Transferase {ECO:0000256|RuleBase:RU361135}.
SQ   SEQUENCE   216 AA;  25496 MW;  67D744CC25B66A31 CRC64;
     MLEIFDVRYD ELTDIRSEDL YKLRKKTFKD RLNWEVNCSN GMEFDEYDNS DTRYLLGIYQ
     GQLICSVRFI ELHLPNMITH TFNALFDDVA LPKRGYIESS RFFVDKTRAK LLFGNHYPIS
     YLFFLSIINY SRHNGYTGIY TIVSRAMLTI LKRSGWQVEV IKEAHITEKE RIYLLHLPID
     RDNQARLLLQ VNQRLQDPCS VLSTWPISLP VMPESA
//

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