ID   GSDM_UNKP               Reviewed;         266 AA.
AC   P0DV52;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   25-MAY-2022, sequence version 1.
DT   03-AUG-2022, entry version 2.
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=Ga0307981_100051429 {ECO:0000303|PubMed:35025633};
OS   Unknown prokaryotic organism.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=2725;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   DOE Joint Genome Institute;
RT   "Saline water microbial communities from Organic Lake, Antarctica - #987.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MASS
RP   SPECTROMETRY.
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]: Precursor of a pore-forming protein
CC       involved in defense against bacteriophages (By similarity). Cleavage of
CC       this precursor by its dedicated protease releases the active moiety
CC       (gasdermin bGSDM, N-terminus) which inserts into membranes, forming
CC       pores and triggering cell death (PubMed:35025633). Expression of bGSDM
CC       and the neighboring protease gene (Ga0307981_100051430) is highly toxic
CC       in E.coli (PubMed:35025633). {ECO:0000250|UniProtKB:A0A0S2DNG5,
CC       ECO:0000269|PubMed:35025633}.
CC   -!- FUNCTION: [Gasdermin bGSDM, N-terminus]: Pore-forming protein that
CC       causes membrane permeabilization via a pyroptosis-like activity. This
CC       is the active form which makes ring-like pores with an interior pore
CC       diameter of 130-190 Angstroms, when integrated in liposomes.
CC       {ECO:0000269|PubMed:35025633}.
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 mediate autoinhibition. The
CC       pyroptosis-like-inducing activity is carried by the released N-terminal
CC       domain (Gasdermin bGSDM, N-terminus). {ECO:0000305|PubMed:35025633}.
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:0000269|PubMed:35025633}.
CC   -!- SUBCELLULAR LOCATION: [Gasdermin bGSDM]: Cytoplasm
CC       {ECO:0000305|PubMed:35025633}.
CC   -!- SUBCELLULAR LOCATION: [Gasdermin bGSDM, N-terminus]: Cell membrane
CC       {ECO:0000269|PubMed:35025633}; Multi-pass membrane protein
CC       {ECO:0000305|PubMed:35025633}. Note=Upon proteolysis the protein forms
CC       membrane-associated puncta. {ECO:0000269|PubMed:35025633}.
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   -!- MASS SPECTROMETRY: Mass=28280.51; Method=Electrospray; Note=Gasdermin
CC       bGSDM, N-terminus.; Evidence={ECO:0000269|PubMed:35025633};
CC   -!- MISCELLANEOUS: Might be a Bacteriodetes scaffold.
CC       {ECO:0000303|PubMed:35025633}.
CC   -!- SIMILARITY: Belongs to the bacterial gasdermin family.
CC       {ECO:0000269|PubMed:35025633}.
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DR   EMBL; SRX5649548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
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 membrane; Cytoplasm; Membrane; Transmembrane;
KW   Transmembrane beta strand.
FT   CHAIN           1..266
FT                   /note="Gasdermin bGSDM"
FT                   /id="PRO_0000455574"
FT   CHAIN           1..247
FT                   /note="Gasdermin bGSDM, N-terminus"
FT                   /evidence="ECO:0000269|PubMed:35025633"
FT                   /id="PRO_0000455575"
FT   REGION          248..266
FT                   /note="C-terminal region"
FT                   /evidence="ECO:0000305|PubMed:35025633"
FT   SITE            247..248
FT                   /note="Cleavage; by protease Ga0307981_100051430"
FT                   /evidence="ECO:0000269|PubMed:35025633"
SQ   SEQUENCE   266 AA;  30335 MW;  8844A94320056029 CRC64;
     MIKYLQSHLE EQGYLFVTLP KPDLAPLQLL TEYKGHLEEY DGSLLDLFEP DGSPFPIRDR
     QLPNFSGQQL LQTDWSAGAD LLHGLFKLFQ QKEDKLKASL SGMKGLVLSF AYENIEEERV
     SEQALDNFLA GAMPKKEGFQ RSVERLQDGE LYVLTSVMRS NQFTVTIDCQ REDQGKLEAA
     VAEIVDAHAS IERKQSNSFS LQTEGEQAFV FACRAAQVLY NKKQWFQFWK KDKDGFRIEK
     REGMVVRGEE DFSVQPLQAP SGLLKL