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OPAM_VIBPA
ID   OPAM_VIBPA              Reviewed;         393 AA.
AC   Q87NA8; Q847W6;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Acyl-homoserine-lactone synthase OpaM;
DE            Short=AHL synthase OpaM;
DE            EC=2.3.1.184;
GN   Name=opaM; OrderedLocusNames=VP1967;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BB22;
RA   Jaques S., McCarter L.L.;
RT   "The opaMN operon of Vibrio parahaemolyticus encodes a homoserine lactone
RT   synthase and autoinducer sensor.";
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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 LuxM / VanM family. {ECO:0000305}.
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DR   EMBL; AY216909; AAO61789.1; -; Genomic_DNA.
DR   EMBL; BA000031; BAC60230.1; -; Genomic_DNA.
DR   RefSeq; NP_798346.1; NC_004603.1.
DR   RefSeq; WP_005481636.1; NC_004603.1.
DR   AlphaFoldDB; Q87NA8; -.
DR   STRING; 223926.28806959; -.
DR   PRIDE; Q87NA8; -.
DR   EnsemblBacteria; BAC60230; BAC60230; BAC60230.
DR   GeneID; 1189478; -.
DR   KEGG; vpa:VP1967; -.
DR   PATRIC; fig|223926.6.peg.1880; -.
DR   eggNOG; ENOG5031MRN; Bacteria.
DR   HOGENOM; CLU_053516_0_0_6; -.
DR   OMA; FWCECEI; -.
DR   Proteomes; UP000002493; Chromosome 1.
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; IPR035304; AHL_synthase.
DR   Pfam; PF17327; AHL_synthase; 1.
PE   3: Inferred from homology;
KW   Autoinducer synthesis; Quorum sensing; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..393
FT                   /note="Acyl-homoserine-lactone synthase OpaM"
FT                   /id="PRO_0000379487"
FT   CONFLICT        80
FT                   /note="D -> H (in Ref. 1; AAO61789)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        94..95
FT                   /note="TV -> IA (in Ref. 1; AAO61789)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        108
FT                   /note="A -> G (in Ref. 1; AAO61789)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        279
FT                   /note="M -> T (in Ref. 1; AAO61789)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   393 AA;  45755 MW;  83F499824B4674F3 CRC64;
     MSLKLSLVSL SNTDLPIETK QQALIDIVLR FLTPQERASL FESITHQRET NLLARYPEYQ
     SKSLSVLFEL MDYRDLVRLD PNNLHDDVYL LELTVAECFP HWLDFWCACE IEAIKQKYSL
     ENREPATELS FEDASYSAML IDDISKSSMR VQLPSYPVAM TLSDAVALSN LELFVQGEKW
     YEILPLLSLS QKGKHFILLQ TQTTPVLVAS ALIQDWNQRN TWLSYAPQFN SEKWRFCLPL
     HGYQELNRLD ILASDLVTDY GSLTVFDQAF QTHITKTEMV CEVLRLTVSG SVQHKLYFLY
     LAQKELMNVL FQSGYKVGFT IIEQAFMLNF YQSIDSKAYF HSGYCDINGD GINTYRGFWN
     FESMVDTFKR TDFRDYKRRI RVIRQNTQVN EHA
 
 
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