GSDM_BRATP
ID GSDM_BRATP Reviewed; 259 AA.
AC P0DV46;
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=Ga0098714_109513 {ECO:0000303|PubMed:35025633};
OS Bradyrhizobium tropiciagri.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=312253;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 28867 / SMS 303 / BR 1009 / SEMIA 6148 / CNPSo 1112;
RX PubMed=26679591; DOI=10.1128/genomea.01482-15;
RA Delamuta J.R., Gomes D.F., Ribeiro R.A., Chueire L.M., Souza R.C.,
RA Almeida L.G., Vasconcelos A.T., Hungria M.;
RT "Genome Sequence of Bradyrhizobium tropiciagri Strain CNPSo 1112T, Isolated
RT from a Root Nodule of Neonotonia wightii.";
RL Genome Announc. 3:0-0(2015).
RN [2] {ECO:0007744|PDB:7N50}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 2-259, FUNCTION, SUBUNIT, DOMAIN,
RP MASS SPECTROMETRY, PALMITOYLATION AT CYS-3, AND MUTAGENESIS OF
RP 234-LEU--PRO-241 AND 238-GLY--SER-259.
RC STRAIN=LMG 28867 / SMS 303 / BR 1009 / SEMIA 6148 / CNPSo 1112;
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 (Ga0098714_109514) is toxic
CC in E.coli on solid medium (PubMed:35025633). Cleavage of this precursor
CC by its dedicated protease releases the active moiety (gasdermin bGSDM,
CC N-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 (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=27552.98; Method=Electrospray; Note=Full-
CC length, unmodified protein expressed in E.coli.;
CC Evidence={ECO:0000269|PubMed:35025633};
CC -!- MASS SPECTROMETRY: Mass=27791.29; Method=Electrospray; Note=Full-
CC length, palmitoylated protein expressed in E.coli.;
CC Evidence={ECO:0000269|PubMed:35025633};
CC -!- MASS SPECTROMETRY: Mass=27817.44; 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; LFLZ01000095.1; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PDB; 7N50; X-ray; 1.67 A; A=2-259.
DR PDBsum; 7N50; -.
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; Transmembrane;
KW Transmembrane beta strand.
FT CHAIN 1..259
FT /note="Gasdermin bGSDM"
FT /id="PRO_0000455564"
FT CHAIN 1..?
FT /note="Gasdermin bGSDM, N-terminus"
FT /evidence="ECO:0000305|PubMed:35025633"
FT /id="PRO_0000455565"
FT REGION 244..259
FT /note="C-terminal region"
FT /evidence="ECO:0000269|PubMed:35025633"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:35025633"
FT MUTAGEN 234..241
FT /note="LKFRGKGP->NRVLGENM: Not cleaved by Runella
FT protease."
FT /evidence="ECO:0000269|PubMed:35025633"
FT MUTAGEN 238..259
FT /note="Missing: Increased cell growth arrest upon
FT induction."
FT /evidence="ECO:0000269|PubMed:35025633"
SQ SEQUENCE 259 AA; 27597 MW; 144585BFCD618F81 CRC64;
MNCSRDTGDE LMAALLAEGI NLILPPRDNI APGDLIIADP QGGARLGGWH EVFNLQLSPE
VATDPGFKSF QFRASSILQV GVAASVMGRV LQALGLGSGS FSSAFSSSNA DTIQLSIVAP
ANKELTNFDA VLVQMNEAKA EPAQGYTDRN FFVVTKVWRA RGIRISVADK SKKQVDLSAK
AVEELTAKAK MELKREDTGS YAFLAASQLI FGLTLREVTY KDGAIVDVAP TGPLKFRGKG
PGDPFAFIGD DAFVDLPES
