GSDM_VITXG
ID GSDM_VITXG Reviewed; 266 AA.
AC A0A2T4VDM4;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-JUL-2018, sequence version 1.
DT 03-AUG-2022, entry version 10.
DE RecName: Full=Gasdermin bGSDM {ECO:0000303|PubMed:35025633};
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=DAT35_31115 {ECO:0000303|Ref.1},
GN Ga0334635_1658 {ECO:0000303|PubMed:35025633};
OS Vitiosangium sp. (strain GDMCC 1.1324).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Archangiaceae; Vitiosangium; unclassified Vitiosangium.
OX NCBI_TaxID=2138576;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GDMCC 1.1324;
RA Lv Y.;
RT "Vitiosangium phaeum 53X41T novel myxobacteria isolated from forest.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:7N51}
RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 2-266, FUNCTION, SUBUNIT, DOMAIN,
RP MASS SPECTROMETRY, PALMITOYLATION AT CYS-4, AND MUTAGENESIS OF
RP 230-PHE--PHE-266.
RC STRAIN=GDMCC 1.1324;
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 (Ga0334635_1659) is toxic in
CC E.coli (PubMed:35025633). Cleavage of this precursor by its dedicated
CC protease releases the active moiety (gasdermin bGSDM, N-terminus) which
CC inserts into membranes, forming pores and triggering cell death (By
CC 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 (Probable). The pyroptosis-like-
CC inducing activity is carried by the released N-terminal domain
CC (Gasdermin bGSDM, N-terminus) (By similarity).
CC {ECO:0000250|UniProtKB:P0DV48, ECO:0000305|PubMed:35025633}.
CC -!- SUBUNIT: [Gasdermin bGSDM]: Monomer in solution.
CC {ECO:0000269|PubMed:35025633}.
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:0000305|PubMed:35025633}.
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:0000269|PubMed:35025633}.
CC -!- PTM: Palmitoylation helps stabilize the inactive state; may self
CC palmitoylate. {ECO:0000269|PubMed:35025633}.
CC -!- MASS SPECTROMETRY: Mass=28320.96; Method=Electrospray; Note=Full-
CC length, unmodified protein expressed in E.coli.;
CC Evidence={ECO:0000269|PubMed:35025633};
CC -!- MASS SPECTROMETRY: Mass=28469.06; Method=Electrospray; Note=Full-
CC length, palmitoylated protein expressed in E.coli.;
CC Evidence={ECO:0000269|PubMed:35025633};
CC -!- MASS SPECTROMETRY: Mass=28494.81; Method=Electrospray; Note=Full-
CC length, modified protein expressed in E.coli.;
CC Evidence={ECO:0000269|PubMed:35025633};
CC -!- SIMILARITY: Belongs to the bacterial gasdermin family.
CC {ECO:0000269|PubMed:35025633}.
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DR EMBL; PZOX01000012; PTL79885.1; -; Genomic_DNA.
DR PDB; 7N51; X-ray; 1.67 A; A=2-266.
DR PDBsum; 7N51; -.
DR SMR; A0A2T4VDM4; -.
DR EnsemblBacteria; PTL79885; PTL79885; DAT35_31115.
DR Proteomes; UP000240889; Unassembled WGS sequence.
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 3D-structure; Antiviral defense; Cell inner membrane; Cell membrane;
KW Cytoplasm; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Transmembrane; Transmembrane beta strand.
FT CHAIN 1..266
FT /note="Gasdermin bGSDM"
FT /id="PRO_0000455576"
FT CHAIN 1..?
FT /note="Gasdermin bGSDM, N-terminus"
FT /evidence="ECO:0000305|PubMed:35025633"
FT /id="PRO_0000455577"
FT REGION 231..266
FT /note="C-terminal region"
FT /evidence="ECO:0000269|PubMed:35025633"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:35025633"
FT MUTAGEN 230..266
FT /note="Missing: Increased cell growth arrest upon
FT induction."
FT /evidence="ECO:0000269|PubMed:35025633"
SQ SEQUENCE 266 AA; 28275 MW; A789A80904209C67 CRC64;
MGLCSDPAIT YLKRLGYNVV RLPREGIQPL HLLGQQRGTV EYLGSLEKLI TQPPSEPPAI
TRDQAAAGIN GQKTENLSFS IGINILKSVL AQFGAGAGIE AQYNQARKVR FEFSNVLADS
VEPLAVGQFL KMAEVDADNP VLKQYVLGNG RLYVITQVIK SNEFTVAAEK SGGGSIQLDV
PEIQKVVGGK LKVEASVSSQ STVTYKGEKQ LVFGFKCFEI GVKNGEITLF ASQPGAIAMA
LDAAGGVMPS DSALLDEGGL LDLEGF
