ID   B5JR98_9BACT            Unreviewed;       603 AA.
AC   B5JR98;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN   ORFNames=VDG1235_190 {ECO:0000313|EMBL:EDY80576.1};
OS   Verrucomicrobiae bacterium DG1235.
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae.
OX   NCBI_TaxID=382464 {ECO:0000313|EMBL:EDY80576.1, ECO:0000313|Proteomes:UP000003839};
RN   [1] {ECO:0000313|EMBL:EDY80576.1, ECO:0000313|Proteomes:UP000003839}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG1235 {ECO:0000313|EMBL:EDY80576.1,
RC   ECO:0000313|Proteomes:UP000003839};
RA   Hart M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073}.
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DR   EMBL; DS990593; EDY80576.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5JR98; -.
DR   eggNOG; COG1404; Bacteria.
DR   HOGENOM; CLU_439181_0_0_0; -.
DR   Proteomes; UP000003839; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.1290; -; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF00082; Peptidase_S8; 2.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003839};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT   DOMAIN          19..215
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          361..499
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   REGION          390..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   603 AA;  64431 MW;  20F011A84F83431E CRC64;
     MITTLLDIDE NVEEYGLNGE GVAIAIIDEG IDYELADFRH PDGSTRIAYA FDLGDDSGSN
     TLNNPIGRGT VYSESEINTA LESQIHLSFY DSFGSSTALA GLAAGKPNES EFSQFQGLAP
     KATLIVVKST FLGLPEDDSA ELNNPTSLYP AIEFVILKAQ ELAMPAVVFV NSRRLEGPTD
     GKSRASELID SYSGANRPRL VFVTSTGDSQ GITNHSLGSI SPGETISLQI DKRQESSLFM
     DLWYPNADSS GDPTPNLKVS ITTPSNTNYG PYGPAVSAGS FFDDQSEPGI ISLFHRSDEF
     DLHRANNGQK EILLLLQGAS GRYSITLTLD PSAKESLPFQ DTLSSNPRTG TNPSEFANFL
     GDGTVSDAAS SANAIVVNGY ANGASWTNLE DQNRADDPAS GTPGNLLTNA NRGQTFDQRD
     VVDFTVPGGG IFGPYPSTSY LSESPANLIK EGSGRYGIAQ ENQAAAALTT GLIALMLQID
     PQLSATEAKD ILRSTATIDD ITDQTPAPEW GSGKLSAPAA LQRTILHSQA LLSPNPIGFA
     SDAGERQIKF KTIPNLRYTL QFRELLEIGD WTDLGTETLG DGGETTFEIP EGHPAGFFRI
     KIR
//