ID   PROT_BRATP              Reviewed;         785 AA.
AC   P0DV47;
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 serine protease Ga0098714_109514 {ECO:0000305};
DE            EC=3.4.21.- {ECO:0000305|PubMed:35025633};
GN   ORFNames=Ga0098714_109514 {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]
RP   FUNCTION.
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: 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 gasdermin
CC       bGSDM and this neighboring protease is toxic in E.coli on solid medium
CC       (PubMed:35025633). {ECO:0000269|PubMed:35025633,
CC       ECO:0000305|PubMed:35025633}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000305}.
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DR   EMBL; LFLZ01000095.1; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   GO; GO:0008236; F:serine-type 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   Gene3D; 1.10.575.10; -; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR008947; PLipase_C/P1_nuclease_dom_sf.
DR   SUPFAM; SSF48537; SSF48537; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
PE   3: Inferred from homology;
KW   Antiviral defense; Hydrolase; Protease; Serine protease.
FT   CHAIN           1..785
FT                   /note="Probable serine protease Ga0098714_109514"
FT                   /id="PRO_0000455583"
FT   REGION          470..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          608..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..628
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   785 AA;  85077 MW;  3B189688DDBF5697 CRC64;
     MTVLDLSYNF ANLSVHDLLE ARDTYHYHLL SKANVVGTAI GLYLIRKDEA WPTRKGEGKT
     PPNKKTYART LSNSEVRDYS WPCILAFVRS WANEDAFGPA GRYDPAQIVP KTLYLADGRA
     VPVCVVQADQ AGSDTSATYS PPGILPAHKL GGGSPIIVRV QGAEYSATAG CLVSDGHLTY
     ALTARHACGE ADTRIFSYLR SGEVEIGASS ANQLTRKPFS EVYPDFPGRR SYVALDVGLV
     RLDQVDDWTS NTYGLPPVGP LGDVHEKNLS LRLIDQPVLG RGATSGLVRG TIKALFYRYR
     SVGGYDYVGD FLISPAEGLA TRHGDSGMVW HLDATTEDDA ANPKPLPKRD LRPLAVAWGG
     QVFEESGVRS AFSIATSLSN VCKLLDVELV TDQSRGVSGY WGRTGHYSIA AFAVALVGDT
     DLRDFLNRNL GILSFDLDTI AEKGFDKSVG QLGDNFVPLA DVPDEIWKKL DHGKNGREGG
     RDVSAGPHGS DGPEHPNHYA DIDGEIGPHK TFRAACLADD SNLTVDAWLQ YYETMAAKAK
     ADGDEDGARR HRNKLKQGLL PFRVWQFFDA MVAFVENKDV VGFLTAAGAA AHYMGDASQP
     LHGSVYSDGD ASRTVTRHHP RTGEDEEVSY GSGVHSAFET AMIADKAAQL FPLIKQELSG
     PGGHALPLLT SGKAMAKATV ELMDKVAGIL EPMRILDSYE QAGAGTRKAT LDGMWKDLGD
     DTAQVMALGA RYLAMLWESA WVHGKGSDIP VRNLTDQNPQ DVRARYIQTS FVPSLTLDKI
     GDELT