ID   ISP_PAEPO               Reviewed;         326 AA.
AC   P29139;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Intracellular serine protease;
DE            EC=3.4.21.-;
GN   Name=isp;
OS   Paenibacillus polymyxa (Bacillus polymyxa).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1406;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 16-35.
RC   STRAIN=72;
RX   PubMed=1834632; DOI=10.1128/jb.173.21.6820-6825.1991;
RA   Takekawa S., Uozumi N., Tsukagoshi N., Udaka S.;
RT   "Proteases involved in generation of beta- and alpha-amylases from a large
RT   amylase precursor in Bacillus polymyxa.";
RL   J. Bacteriol. 173:6820-6825(1991).
CC   -!- FUNCTION: Involved in the generation of beta- and alpha-amylases from
CC       the large amylase precursor.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; D00862; BAA00735.1; -; Genomic_DNA.
DR   PIR; C41335; C41335.
DR   AlphaFoldDB; P29139; -.
DR   SMR; P29139; -.
DR   MEROPS; S08.030; -.
DR   eggNOG; COG1404; Bacteria.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07477; Peptidases_S8_Subtilisin_subset; 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; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR034202; Subtilisin_Carlsberg-like.
DR   PANTHER; PTHR43399:SF5; CELL WALL-ASSOCIATED PROTEASE; 1.
DR   PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Protease; Serine protease.
FT   CHAIN           1..326
FT                   /note="Intracellular serine protease"
FT                   /id="PRO_0000076409"
FT   DOMAIN          23..303
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        49
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        86
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        244
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   326 AA;  35174 MW;  8DD2C7C910370F13 CRC64;
     MERKVHIIPY QVIKQEQQVN EIPRGVEMIQ APAVWNQTRG RGVKVAVLDT GCDADHPDLK
     ARIIGGRNFT DDDEGDPEIF KDYNGHGTHV AGTIAATENE NGVVGVAPEA DLLIIKVLNK
     QGSGQYDWII QGIYYAIEQK VDIISMSLGG PEDVPELHEA VKKAVASQIL VMCAAGNEGD
     GDDRTDELGY PGCYNEVISV GAINFDRHAS EFSNSNNEVD LVAPGEDILS TVPGGKYATF
     SGTSMATPHV AGALALIKQL ANASFERDLT EPELYAQLIK RTIPLGNSPK MEGNGLLYLT
     AVEELSRIFD TQRVAGILST ASLKVK
//