ID   PROT_DESBX              Reviewed;         820 AA.
AC   P0DV51;
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=Probable protease Ga0182885_104520 {ECO:0000305};
DE            EC=3.4.-.- {ECO:0000305|PubMed:35025633};
GN   ORFNames=Ga0182885_104520 {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, AND FUNCTION.
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: Probably a dedicated protease for substrate gasdermin bGSDM;
CC       cleaves the bGSDM precursor, releasing the pore-forming moiety, which
CC       integrates into the membrane and triggers cell death. Involved in
CC       defense against bacteriophages (Probable). Expression of bacterial
CC       gasdermin (bGSDM) and this neighboring protease is toxic in E.coli
CC       (PubMed:35025633). {ECO:0000269|PubMed:35025633,
CC       ECO:0000305|PubMed:35025633}.
CC   -!- SIMILARITY: Belongs to the peptidase C25 family. {ECO:0000305}.
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DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR029030; Caspase-like_dom_sf.
DR   SUPFAM; SSF52129; SSF52129; 1.
PE   3: Inferred from homology;
KW   Antiviral defense; Hydrolase; Protease.
FT   CHAIN           1..820
FT                   /note="Probable protease Ga0182885_104520"
FT                   /id="PRO_0000455586"
SQ   SEQUENCE   820 AA;  90862 MW;  41251E1E5C405AFF CRC64;
     MQNWALVIGI NRYWRADACL KGAVKDALKM REWLTSIDGG AVPSRNLILL LSPHDDPESC
     GGASALPATQ DMIIQAIEQI FRKSGEEGDR FFFYYSGHGL TARMSFSNES GIIPNDFSDT
     LTNKALSLRS IFERFQSTRF REQFFFIDAC RNIPWEGERE FLISQYPLPK PPKPPVFPQF
     IMYATSPGVK AVEIHEAGNE RGAFTDALLA GLRGTGNAKL WHEEDREYMV RWDNLFRFVE
     EEVIRRRLSV SENRVPPLIQ EPRQFGERGS CNPTLASLPA EVFPEVSLDV HLDPMTVASQ
     TEVIVGDLGG VLRREFPVTA LPVHFDLQPR TYSIRTSTPD FRSEKRYYQV DLYGPAEVSI
     KMVPGTGYST PVSPSSGVSK SVDGNTATAS VLMRSHDPLA YLELLDNSGT TIETGIGQIY
     RPRVKPGFYR LRLRTPEGIP HERLVELSSG ESADITLDAP PQTDSGLFTH IAFTSHMYQG
     EPNIIQPSEA IGPAQSMHLS TILALAGGAV NEDSSYGGKL RGLGITSFRN IAGEEATSGM
     QILFGNEVTA PAFTDNYLSA VRLRCWGIDR GIPAEYRQPL HVADITGLAQ ATWEMEPGSY
     LLSIELPDRM PVVFPVAALS NRLSLLVVTQ DATGVVNFFR YLPSLKDELP GDPRYEAARF
     PVLRRLEYIQ RSCMVGRFEQ AYQNARELLN AKWIDPMAGL LGSYLLMRLG KSDELCIPAR
     NLSECFGELS DSHVIAAEYE AGIGNEEKAA DAFRRALDNG LPIMSDCLTK LIYGMERYGI
     EHPRAALAKS YYSHGIKGLL WSACPRKACE AAPGETGADA