GSDM_GILLR
ID GSDM_GILLR Reviewed; 266 AA.
AC H2BXL6;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 20.
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=Gilli_2518 {ECO:0000303|PubMed:23450183};
OS Gillisia limnaea (strain DSM 15749 / LMG 21470 / R-8282).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Gillisia.
OX NCBI_TaxID=865937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15749 / LMG 21470 / R-8282;
RX PubMed=23450183; DOI=10.4056/sigs.3216895;
RA Riedel T., Held B., Nolan M., Lucas S., Lapidus A., Tice H., Del Rio T.G.,
RA Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S., Liolios K.,
RA Mavromatis K., Pagani I., Ivanova N., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Rohde M., Tindall B.J., Detter J.C., Goker M.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Woyke T.;
RT "Genome sequence of the Antarctic rhodopsins-containing flavobacterium
RT Gillisia limnaea type strain (R-8282(T)).";
RL Stand. Genomic Sci. 7:107-119(2012).
RN [2]
RP FUNCTION, MASS SPECTROMETRY, AND MUTAGENESIS OF 228-PHE--LYS-235.
RC STRAIN=DSM 15749 / LMG 21470 / R-8282;
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 (Gilli_2517) is not 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 mediate autoinhibition. The
CC pyroptosis-like-inducing activity is carried by the released N-terminal
CC domain (Gasdermin bGSDM, 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 -!- MASS SPECTROMETRY: Mass=29724.43; Method=Electrospray; Note=Full-
CC length, unmodified 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; JH594606; EHQ03140.1; -; Genomic_DNA.
DR RefSeq; WP_006989447.1; NZ_JH594606.1.
DR STRING; 865937.Gilli_2518; -.
DR EnsemblBacteria; EHQ03140; EHQ03140; Gilli_2518.
DR eggNOG; ENOG5033MVA; Bacteria.
DR HOGENOM; CLU_1044940_0_0_10; -.
DR Proteomes; UP000003844; 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 Antiviral defense; Cell inner membrane; Cell membrane; Cytoplasm; Membrane;
KW Reference proteome; Transmembrane; Transmembrane beta strand.
FT CHAIN 1..266
FT /note="Gasdermin bGSDM"
FT /id="PRO_0000455568"
FT CHAIN 1..?
FT /note="Gasdermin bGSDM, N-terminus"
FT /id="PRO_0000455569"
FT REGION ?..266
FT /note="C-terminal region"
FT /evidence="ECO:0000305"
FT MUTAGEN 228..235
FT /note="FFKKGDAK->NRVLGENM: Not cleaved by Runella
FT protease."
FT /evidence="ECO:0000269|PubMed:35025633"
SQ SEQUENCE 266 AA; 29769 MW; 8A61237B21CA04A3 CRC64;
MSKVLKNALA GYGYNLVALP KEGIAPLLLL YKNKRDVSSS GNNIDKLFAL ADSPPPIVSK
NNATLNLQQN STVSFDGKAG VDILDWLLQK LKMGKLRGNI NADHINSLQI SYQNVFEDNV
SLLQLDNFIS GSEPKVDQFN TFKEKLKDNE LFVINSVLKS NSFSVSAQNK NGQNIDLEAT
IKGIVDADVN VGRSKKDEVL MEYKNATPIV FAFKAQKIIY DHKKWWQFFK KGDAKFRIKD
EHGVVLKDES GFPTQSLEET NELINI
