GSDM_DESBX
ID GSDM_DESBX Reviewed; 266 AA.
AC P0DV50;
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=Ga0182885_104519 {ECO:0000303|PubMed:35025633};
OS Desulfuromonadales bacterium.
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales.
OX NCBI_TaxID=2099678;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bin 1;
RX PubMed=29996505; DOI=10.3390/microorganisms6030065;
RA Toth C.R.A., Berdugo-Clavijo C., O'Farrell C.M., Jones G.M., Sheremet A.,
RA Dunfield P.F., Gieg L.M.;
RT "Stable Isotope and Metagenomic Profiling of a Methanogenic Naphthalene-
RT Degrading Enrichment Culture.";
RL Microorganisms 6:0-0(2018).
RN [2]
RP IDENTIFICATION, FUNCTION, AND MUTAGENESIS OF 240-MET--PRO-247.
RC STRAIN=Bin 1;
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). Expression
CC of bGSDM and the neighboring protease gene (Ga0182885_104520) is toxic
CC in E.coli (PubMed:35025633). Cleavage of this precursor by its
CC dedicated protease releases the active moiety (gasdermin bGSDM, N-
CC terminus) which inserts into membranes, forming pores and triggering
CC cell death (By similarity). {ECO:0000250|UniProtKB:A0A0S2DNG5,
CC ECO:0000250|UniProtKB:P0DV48, 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 -!- SIMILARITY: Belongs to the bacterial gasdermin family.
CC {ECO:0000269|PubMed:35025633}.
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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; Transmembrane; Transmembrane beta strand.
FT CHAIN 1..266
FT /note="Gasdermin bGSDM"
FT /id="PRO_0000455566"
FT CHAIN 1..?
FT /note="Gasdermin bGSDM, N-terminus"
FT /evidence="ECO:0000305|PubMed:35025633"
FT /id="PRO_0000455567"
FT REGION ?..266
FT /note="C-terminal region"
FT /evidence="ECO:0000305"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P0DV46"
FT MUTAGEN 240..247
FT /note="MKALGKAP->NRVLGENM: Not cleaved by Runella
FT protease."
FT /evidence="ECO:0000269|PubMed:35025633"
SQ SEQUENCE 266 AA; 28618 MW; 398E93091AE5258D CRC64;
MWCKDPFLTY LKEFGYNVIR LPKADVKPLQ VLARCGKDLN RLGEINNLLV AGDSIPLPRL
KENTRAASIS GQRTGDLSVG VGLSILGTVL GAMGGSKLGL DTKYQNAKTT MFEFQDVFED
TVEIIELDKF LGDADINPFS RHVAELLEAD DLYITTSTIK STKFTIEAKK SDGTALELTI
PDIQGIVGGN VKVSGAASVT SKICYESPIP LVFGFQAVRL FYDNGRYTAI EPLDSGSAGM
KALGKAPSDG AARLMTDGPF LRLTGV
