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GSDM_LYSEN
ID   GSDM_LYSEN              Reviewed;         271 AA.
AC   A0A0S2DNG5;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   17-FEB-2016, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=Gasdermin bGSDM {ECO:0000305};
DE            Short=bGSDM {ECO:0000303|PubMed:35025633};
DE   AltName: Full=Bacterial gasdermin {ECO:0000303|PubMed:35025633};
DE   Contains:
DE     RecName: Full=Gasdermin bGSDM, N-terminus {ECO:0000305};
GN   ORFNames=FE772_23055 {ECO:0000303|PubMed:31540995},
GN   Ga0399710_4913 {ECO:0000303|PubMed:35025633},
GN   GLE_4743 {ECO:0000303|PubMed:26597042};
OS   Lysobacter enzymogenes.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=69;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C3;
RX   PubMed=26597042; DOI=10.1186/s12864-015-2191-z;
RA   de Bruijn I., Cheng X., de Jager V., Exposito R.G., Watrous J., Patel N.,
RA   Postma J., Dorrestein P.C., Kobayashi D., Raaijmakers J.M.;
RT   "Comparative genomics and metabolic profiling of the genus Lysobacter.";
RL   BMC Genomics 16:991-991(2015).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YC36;
RX   PubMed=31540995; DOI=10.1128/aem.01742-19;
RA   Feng T., Han Y., Li B., Li Z., Yu Y., Sun Q., Li X., Du L., Zhang X.H.,
RA   Wang Y.;
RT   "Interspecies and Intraspecies Signals Synergistically Regulate Lysobacter
RT   enzymogenes Twitching Motility.";
RL   Appl. Environ. Microbiol. 85:0-0(2019).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-7.
RC   STRAIN=YC36;
RX   PubMed=35025633; DOI=10.1126/science.abj8432;
RA   Johnson A.G., Wein T., Mayer M.L., Duncan-Lowey B., Yirmiya E.,
RA   Oppenheimer-Shaanan Y., Amitai G., Sorek R., Kranzusch P.J.;
RT   "Bacterial gasdermins reveal an ancient mechanism of cell death.";
RL   Science 375:221-225(2022).
CC   -!- FUNCTION: [Gasdermin bGSDM]: Involved in defense against
CC       bacteriophages. When this probable 4 gene operon (bGSDM-FE772_23060-
CC       FE772_23065-FE772_23070) is inserted into E.coli it provides nearly
CC       100-fold protection against phages T5 and T6 and about 8-fold against
CC       phage T4. The operon without bGSDM no longer protects against phage
CC       (PubMed:35025633). Cleavage of this precursor by its dedicated
CC       protease(s) releases the active moiety (gasdermin bGSDM, N-terminus)
CC       which inserts into membranes, forming pores and triggering cell death
CC       (By similarity). {ECO:0000250|UniProtKB:P0DV48,
CC       ECO:0000269|PubMed:35025633}.
CC   -!- FUNCTION: [Gasdermin bGSDM, N-terminus]: Pore-forming protein that
CC       causes membrane permeabilization via a pyroptosis-like activity. Makes
CC       ring-like pores when released. {ECO:0000250|UniProtKB:P0DV48}.
CC   -!- ACTIVITY REGULATION: [Gasdermin bGSDM]: The full-length protein before
CC       cleavage is inactive: intramolecular interactions between the N-
CC       terminal domain and the C-terminal region as well as the lipid
CC       modification, mediate autoinhibition. The pyroptosis-like-inducing
CC       activity is carried by the released N-terminal domain (Gasdermin bGSDM,
CC       N-terminus). {ECO:0000250|UniProtKB:P0DV48}.
CC   -!- SUBUNIT: [Gasdermin bGSDM]: Monomer. {ECO:0000250|UniProtKB:P0DV48}.
CC   -!- SUBUNIT: [Gasdermin bGSDM, N-terminus]: Forms large, probably
CC       homooligomeric ring-shaped pores when inserted in membranes.
CC       {ECO:0000250|UniProtKB:P0DV48}.
CC   -!- SUBCELLULAR LOCATION: [Gasdermin bGSDM]: Cytoplasm
CC       {ECO:0000250|UniProtKB:P0DV48}.
CC   -!- SUBCELLULAR LOCATION: [Gasdermin bGSDM, N-terminus]: Cell inner
CC       membrane {ECO:0000250|UniProtKB:P0DV48}; Multi-pass membrane protein
CC       {ECO:0000305}.
CC   -!- DOMAIN: The N-terminus has marked structural similarity to the
CC       mammalian gasdermin N-terminal domain. The C-terminal region wraps
CC       around the twisted beta sheet core, probably stabilizing the inactive
CC       state. {ECO:0000250|UniProtKB:P0DV48}.
CC   -!- PTM: Palmitoylation helps stabilize the inactive state; may self
CC       palmitoylate. {ECO:0000250|UniProtKB:P0DV46}.
CC   -!- DISRUPTION PHENOTYPE: When deleted from its operon, no longer protects
CC       E.coli against bacteriophages T4, T5 or T6.
CC       {ECO:0000269|PubMed:35025633}.
CC   -!- SIMILARITY: Belongs to the bacterial gasdermin family.
CC       {ECO:0000269|PubMed:35025633}.
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DR   EMBL; CP013140; ALN60084.1; -; Genomic_DNA.
DR   EMBL; CP040656; QCW28095.1; -; Genomic_DNA.
DR   RefSeq; WP_057949280.1; NZ_CP040656.1.
DR   EnsemblBacteria; ALN60084; ALN60084; GLE_4743.
DR   KEGG; lez:GLE_4743; -.
DR   PATRIC; fig|69.6.peg.4677; -.
DR   OMA; TQRDEVE; -.
DR   OrthoDB; 1715617at2; -.
DR   Proteomes; UP000061569; Chromosome.
DR   Proteomes; UP000308311; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antiviral defense; Cell inner membrane; Cell membrane; Cytoplasm;
KW   Lipoprotein; Membrane; Palmitate; Reference proteome; Transmembrane;
KW   Transmembrane beta strand.
FT   CHAIN           1..271
FT                   /note="Gasdermin bGSDM"
FT                   /id="PRO_0000455570"
FT   CHAIN           1..?
FT                   /note="Gasdermin bGSDM, N-terminus"
FT                   /id="PRO_0000455571"
FT   REGION          ?..271
FT                   /note="C-terminal region"
FT                   /evidence="ECO:0000305"
FT   LIPID           7
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P0DV46"
FT   MUTAGEN         7
FT                   /note="C->A: 4-gene operon still protects against phage."
FT                   /evidence="ECO:0000269|PubMed:35025633"
SQ   SEQUENCE   271 AA;  28450 MW;  098999A7443A0A8D CRC64;
     MSILPGCKDP SLSALKSKGY NVVQLPRADL RPTQLLVEKS KRLQRLGELL SVFDAAADGP
     PAPPVSADRP GPNIAGTQSA DLDVDLGLSV LRGIISALGG STLGVDAAFA RAATVQFEFS
     STLENNSELA LIDRFLAASR VNPHARAVAE MLEQDQVYVV TSTLKAQRIN VAAKDSNKQS
     LGLNLPVIQD AIGANVKIAA AAASGSTVSF EGAVPLVFGF QAVRLIFEQG RYRTMRLVDA
     GGVVAEAVRP DGAADGEPPC YLDVEAMLLD R
 
 
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