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PVDQ_PSEU2
ID   PVDQ_PSEU2              Reviewed;         779 AA.
AC   Q4ZV08;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Acyl-homoserine lactone acylase PvdQ;
DE            Short=AHL acylase PvdQ;
DE            Short=Acyl-HSL acylase PvdQ;
DE            EC=3.5.1.97;
DE   Contains:
DE     RecName: Full=Acyl-homoserine lactone acylase PvdQ subunit alpha;
DE              Short=Acyl-HSL acylase PvdQ subunit alpha;
DE   Contains:
DE     RecName: Full=Acyl-homoserine lactone acylase PvdQ subunit beta;
DE              Short=Acyl-HSL acylase PvdQ subunit beta;
DE   Flags: Precursor;
GN   Name=pvdQ; OrderedLocusNames=Psyr_1971;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT   syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
CC   -!- FUNCTION: Catalyzes the deacylation of acyl-homoserine lactone (AHL or
CC       acyl-HSL), releasing homoserine lactone (HSL) and the corresponding
CC       fatty acid. Possesses a specificity for the degradation of long-chain
CC       acyl-HSLs (side chains of 11 to 14 carbons in length) (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acyl-L-homoserine lactone + H2O = a carboxylate + L-
CC         homoserine lactone; Xref=Rhea:RHEA:18937, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:55474, ChEBI:CHEBI:58633; EC=3.5.1.97;
CC   -!- SUBUNIT: Heterodimer of an alpha subunit and a beta subunit processed
CC       from the same precursor. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- MISCELLANEOUS: AHL-mediated signaling mediates quorum sensing in many
CC       species of Proteobacteria, regulating hundreds of genes, including many
CC       that code for extracellular virulence factors.
CC   -!- SIMILARITY: Belongs to the peptidase S45 family. {ECO:0000305}.
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DR   EMBL; CP000075; AAY37014.1; -; Genomic_DNA.
DR   RefSeq; WP_011267358.1; NC_007005.1.
DR   RefSeq; YP_235052.1; NC_007005.1.
DR   AlphaFoldDB; Q4ZV08; -.
DR   SMR; Q4ZV08; -.
DR   STRING; 205918.Psyr_1971; -.
DR   MEROPS; S45.004; -.
DR   EnsemblBacteria; AAY37014; AAY37014; Psyr_1971.
DR   KEGG; psb:Psyr_1971; -.
DR   PATRIC; fig|205918.7.peg.2013; -.
DR   eggNOG; COG2366; Bacteria.
DR   HOGENOM; CLU_017615_0_0_6; -.
DR   OMA; QGIPWVN; -.
DR   BRENDA; 3.5.1.97; 5193.
DR   Proteomes; UP000000426; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR   GO; GO:0009372; P:quorum sensing; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1400.10; -; 1.
DR   Gene3D; 1.10.439.10; -; 1.
DR   Gene3D; 2.30.120.10; -; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR043147; Penicillin_amidase_A-knob.
DR   InterPro; IPR023343; Penicillin_amidase_dom1.
DR   InterPro; IPR043146; Penicillin_amidase_N_B-knob.
DR   InterPro; IPR002692; S45.
DR   PANTHER; PTHR34218; PTHR34218; 1.
DR   Pfam; PF01804; Penicil_amidase; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Periplasm; Quorum sensing; Signal; Zymogen.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..779
FT                   /note="Acyl-homoserine lactone acylase PvdQ"
FT                   /id="PRO_0000253373"
FT   CHAIN           26..?201
FT                   /note="Acyl-homoserine lactone acylase PvdQ subunit alpha"
FT                   /id="PRO_0000253374"
FT   PROPEP          ?202..223
FT                   /note="Spacer peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000253375"
FT   CHAIN           224..779
FT                   /note="Acyl-homoserine lactone acylase PvdQ subunit beta"
FT                   /id="PRO_0000253376"
FT   REGION          731..750
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        224
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   779 AA;  84673 MW;  7DCDEFC186736830 CRC64;
     MIISRPLCSF VFAGLSFAVI LPAQALVEPG NQAARAEIRR TGFGVPHIVA ANERGLGYGI
     GYAYAQDNLC LLANEVVTVN GQRSRYFGPD KATLEQRNNM ASDLLFQWLN TPQALADFWN
     AQPREIRQLM QGYVAGYNRS LAEQTTQGLP QPCAAEWVRP ISTDDLLRLT RRLLVEGGVG
     QFAEALAGAT PPAQQKPLQV DAQQAQALQL AAARNQRFAL ERGSNAVAIG RELSANGRGM
     LLANPHFPWG GGMRFYQMHL TIPGKLDVMG AALPGLPLIN IGFNQHLAWS HTVDTSKHFT
     LHRLQLDPKD STRYLLDGQS VAMGKQQVSV DVKQADGSLK SVPRIVYSSI FGPVVQWPGK
     LDWDSKFAFS LRDANLQNDR VLQQWYAMDK ADSLKAFQDS VRKIQGIPWV NTLAVDAQGQ
     ALYMNLSVVP NVDAARLARC SDPRIGTELI VLDGSRSECN WEVSAEAAQA GIYPSSRQPQ
     LLRTDFVQHS NDSAWMVNPA APLQGFSPLI SQDGQPLGQR ARFALDRLES LKTAGKISVE
     NLQAMVMDNE VYQAGQVLPD LLTFCASELG DDAARLAPLC AALKDWDGRA DLNSGIGFVY
     FQKIMTSMQA VASRWRVAFD PQDPVHTPSG LAIENPSVAT ALRAAMLAAV DDVAKAGLPA
     GSKWGDIQVS SISGKQIPIH GGPAGLGVYN AMQTVAGKDG KREVVSGTSY LQVVTFDEQG
     PKAQGLLAFS ESSNPQSAHS SDQTEAFSKK QWQALPFTEQ QIKADPAYEV QVISEEPDR
 
 
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