ID   PROT_UNKP               Reviewed;        1062 AA.
AC   P0DV53;
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=Roc-COR-CHAT protease {ECO:0000303|PubMed:35025633};
DE            EC=3.4.21.- {ECO:0000305|PubMed:35025633};
DE   AltName: Full=Protease Ga0307981_100051430 {ECO:0000305};
GN   ORFNames=Ga0307981_100051430 {ECO:0000303|PubMed:35025633};
OS   Unknown prokaryotic organism.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=2725;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   DOE Joint Genome Institute;
RT   "Saline water microbial communities from Organic Lake, Antarctica - #987.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
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: A dedicated protease for substrate gasdermin bGSDM; cleaves
CC       the bGSDM precursor, releasing the pore-forming moiety, which
CC       integrates into the membrane and triggers cell death. Probably involved
CC       in defense against bacteriophages. Expression of bGSDM and this
CC       neighboring protease is highly toxic in E.coli.
CC       {ECO:0000269|PubMed:35025633}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Active between pH 6.0 and 10.2. {ECO:0000269|PubMed:35025633};
CC   -!- MISCELLANEOUS: Might be a Bacteriodetes scaffold.
CC       {ECO:0000303|PubMed:35025633}.
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DR   EMBL; SRX5649548; -; 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; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR032171; COR.
DR   InterPro; IPR045439; EAD11.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF16095; COR; 1.
DR   Pfam; PF19964; EAD11; 1.
DR   SMART; SM00369; LRR_TYP; 3.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51450; LRR; 6.
PE   1: Evidence at protein level;
KW   Antiviral defense; Hydrolase; Leucine-rich repeat; Protease; Repeat;
KW   Serine protease.
FT   CHAIN           1..1062
FT                   /note="Roc-COR-CHAT protease"
FT                   /id="PRO_0000455580"
FT   REPEAT          70..94
FT                   /note="LRR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          95..116
FT                   /note="LRR 2"
FT                   /evidence="ECO:0000305"
FT   REPEAT          115..141
FT                   /note="LRR 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          142..159
FT                   /note="LRR 4"
FT                   /evidence="ECO:0000305"
FT   REPEAT          160..180
FT                   /note="LRR 5"
FT                   /evidence="ECO:0000305"
FT   REPEAT          181..203
FT                   /note="LRR 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          204..226
FT                   /note="LRR 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          228..249
FT                   /note="LRR 8"
FT                   /evidence="ECO:0000255"
FT   REGION          836..856
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        931
FT                   /evidence="ECO:0000250|UniProtKB:P0DV49"
FT   ACT_SITE        980
FT                   /evidence="ECO:0000250|UniProtKB:P0DV49"
SQ   SEQUENCE   1062 AA;  122028 MW;  67AD9BBB23E81EE0 CRC64;
     MPQPAIIAKL EQQLRITIAP FDAPDLKAFM RYGRKGDDNS QYFLKDGKLT GLKLRTLGLK
     DTSFLEEREL AGLQGLYLAE NDFSSLQLPG HLQQLRLLHL ADNKELKTLE FAGSMPLLEE
     IDLSDSGIQT LQLPACPALQ KLDVSRSKLE AFSFASACPA LWWLDLSGNG ELRKLKMPAG
     FKALQYLYLY KSGIQELQIN GKLPKLVVLD LEGNQLKQWP EKLLLPEGLE TLYLEGNPIE
     NIPETIRGSG ERHNSVEDVR QYLLSIIDED KVEYLHQAKM ILVGNGEVGK TSIRLKLLDS
     KATLPKKKDR TQGLDIVPYE LKALSPDLTG LEDAIDFQLN IWDFGGQGKY REVQQLFFSP
     QSLYLFVTAC DDTPEDKESY VTFDYWMSLV HALSYDREQE RSSPVIHVVN KIDKERMDID
     QTAHNRFGNV EEFHAISCKH LTNFEALRKA IPRVLPKVGQ GIFRDQYNED WLGVMEELQR
     RQGEHHITYQ EYRDEVCKDR LNDGEARAWL RILDRIGTVI YFGENEKLKD WIILNPNWVK
     QAVFEVIDSG ERNPVPQWRF EKQIWSHYSE KEREKLFELL QAYDLAYKQQ NAFGEQEFVV
     PALLEHESPN YQDLLPQEEL PLKLRFAFKP ILPAGTVNKL MVRLKDYIYR GLMWKDNVVF
     HHPDSNAYVQ VEEDWQEHFI YLSVYGKQPS VIYETVTSTL KDINNDFKNA KFLKELEFTV
     EGFDGEEWMK KRLLKKAGAD FFNFLWEKPG IHYKEEDEKN IMDQVKELIA KNRVGDALEM
     LKSLVPAHLE AEVLQLISRY SKLQRDSRMG ILANNDENVE RNRIVSSILN LASEAERDND
     HTGLSDSSDQ EDETFTNVTD QTKKILFICS SPSGKNLLDF GKEFKSIGIA RQLADSRDDY
     AEPIIKTSVE ADDLLHIMTK YQPDILHISL HSSKSKGLYF ENNAGQAEPI SAEDFKDIIE
     TYASDPDGKG RIETIVLSCC DSEAYGRAIT NFADHIVVTK DLFPDKAAVV YAKDFYRMLF
     NNKDIGFAHR SATSAIKRKK YPSDGFAHPI HEIPFLIKND DK