ID   PROT_RUNZN              Reviewed;         927 AA.
AC   P0DV49;
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:0000269|PubMed:35025633};
DE   AltName: Full=Protease G563DRAFT_02009 {ECO:0000305};
GN   ORFNames=G563DRAFT_02009 {ECO:0000303|PubMed:35025633};
OS   Runella zeae (strain ATCC BAA-293 / DSM 19591 / LMG 21438 / NS12).
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Spirosomaceae; Runella.
OX   NCBI_TaxID=1123078;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-293 / DSM 19591 / LMG 21438 / NS12;
RA   Kyrpides N., Huntemann M., Han J., Chen A., Mavromatis K., Markowitz V.,
RA   Palaniappan K., Ivanova N., Schaumberg A., Pati A., Liolios K.,
RA   Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, PROBABLE ACTIVE SITE, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND MUTAGENESIS OF HIS-796 AND CYS-840.
RC   STRAIN=ATCC BAA-293 / DSM 19591 / LMG 21438 / NS12;
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 gasdermin bGSDM; cleaves the bGSDM
CC       precursor, releasing the pore-forming moiety, which integrates into the
CC       membrane and triggers cell death (PubMed:35025633). Probably involved
CC       in defense against bacteriophages (Probable). Expression of bGSDM and
CC       this neighboring protease is highly toxic in E.coli. Cells expressing
CC       the gene pair stop dividing and lose membrane integrity. Both proteins
CC       are required to kill E.coli. The bGSDM recognition site is larger than
CC       the 8 residues surrounding the cleavage site; replacement of the
CC       endogenous recognition site by the Runella site (NRVLGENM) in a number
CC       of other bGSDMs is not sufficient for them to be cleaved
CC       (PubMed:35025633). {ECO:0000269|PubMed:35025633,
CC       ECO:0000305|PubMed:35025633}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.4 to 10.2. {ECO:0000269|PubMed:35025633};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AUIF01000011; -; 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; IPR032675; LRR_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF16095; COR; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   Antiviral defense; Hydrolase; Leucine-rich repeat; Protease; Repeat;
KW   Serine protease.
FT   CHAIN           1..927
FT                   /note="Roc-COR-CHAT protease"
FT                   /id="PRO_0000455579"
FT   REPEAT          38..61
FT                   /note="LRR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          83..107
FT                   /note="LRR 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          109..125
FT                   /note="LRR 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          127..151
FT                   /note="LRR 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          171..194
FT                   /note="LRR 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          195..217
FT                   /note="LRR 7"
FT                   /evidence="ECO:0000255"
FT   REGION          152..170
FT                   /note="LRR 5"
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        796
FT                   /evidence="ECO:0000305|PubMed:35025633"
FT   ACT_SITE        840
FT                   /evidence="ECO:0000305|PubMed:35025633"
FT   MUTAGEN         796
FT                   /note="H->A: Protease-bGSDM pair no longer toxic in E.coli,
FT                   protease does not cleave bGSDM, liposomes incubated with
FT                   bGSDM do not leak."
FT                   /evidence="ECO:0000269|PubMed:35025633"
FT   MUTAGEN         840
FT                   /note="C->A: Protease-bGSDM pair no longer toxic in E.coli,
FT                   protease does not cleave bGSDM, liposomes incubated with
FT                   bGSDM do not leak."
FT                   /evidence="ECO:0000269|PubMed:35025633"
SQ   SEQUENCE   927 AA;  106337 MW;  BE6A48B0BA9BB6BC CRC64;
     MSTLNNLTKT LTQQVDDGPI SAVRLVKGYD NSYALNAAGQ VTALSIGNSS LKKLVLGTEA
     QALEYLYLSG SESLKEVVFE VPLPHLTHLY LNNCAIKDIT IPKGFRSLQQ VYLQKNGLTE
     LVFEGDCPAL VLLDVSENQL KGLSFHSGFR ALKYIYATNN VLQKITFNRS MRLLNTLHLA
     KNQLTELAPF LSEIETMETL YLQGNQLLRI DREIWDRDLN CWDTMKGYLT SLNKGNIIRE
     YLHEAKMILI GNGEVGKTSI RLKLLDINAP LPDKKDRTPG LDIVPYTIAN LSSAQTGLPA
     STSFTFNIWD FGGQGKYREI QQLFCSRKSL YLYVTAYDDT ADYNELYVGY EYWLAMANAY
     NNDSGQHSPV IYVQNKNDMG EKPINEEEVK HKFGNVGAFI KISCVDKEQF TALPKLIVKS
     ISKISEDIFT VQYNSEWLGV KEDLNELKNQ GTNYISKEEF ITICTERGLS EDEIRAWLTV
     LDRIGAVIYF GDNEKLKDWI VLNPIWVKDA ICKVIDFEFY DDIATLKPSF LPKIWEEYSE
     SEREKLLQLL ISYHFCYKEE ESFIVPALFT ENQPKYPEHL SSFDCEIKLK YVSFLPAGTL
     HKFMVKLHDK IYNELRWKKG VVLQDGATNT YAEVTERWKE HSIYIRLKDK KGQHPLWQEI
     QKTLQELNEE LKTTKLMQLD FEVYCFYNNK WKAKPDIEDL CELDSTNIFK FMFGLSSPVK
     EYISQKPTPL LGKAKLSIIF LTADPENKNP IGASVQKQRI ENTISDAFEF YNNLETKYNE
     IGSNTVGKDI VHITVHGIPD QLFFVHDKHT DQSNPVQSDY LCKQLEKTKQ VKKLIVLIAC
     NSETTAKKIV DGGLTKYAIG TTIDISSKAA IDFSEKFYDL LKNSPLQIES VFEETCYELN
     QDKYRAKLDD GEFYDYSKVF KIFKKTT