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BPRX_DICNO
ID   BPRX_DICNO              Reviewed;         595 AA.
AC   P42780;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Extracellular subtilisin-like protease;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
OS   Dichelobacter nodosus (Bacteroides nodosus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales;
OC   Cardiobacteriaceae; Dichelobacter.
OX   NCBI_TaxID=870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Good R.T., Brandon R.B., Langford C.J., Moses E.K.;
RT   "The cloning, nucleotide sequence and expression of a structural gene
RT   encoding a member of a family of extracellular proteases from Dichelobacter
RT   nodosus.";
RL   Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; L08175; AAA99869.1; -; Genomic_DNA.
DR   RefSeq; WP_012030937.1; NZ_SRJB01000002.1.
DR   AlphaFoldDB; P42780; -.
DR   SMR; P42780; -.
DR   MEROPS; S08.023; -.
DR   PATRIC; fig|870.4.peg.318; -.
DR   OMA; ESVENDM; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07496; Peptidases_S8_13; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR002884; P_dom.
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; IPR034176; Peptidases_S8_13.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51829; P_HOMO_B; 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   3: Inferred from homology;
KW   Hydrolase; Protease; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..130
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000027001"
FT   CHAIN           131..595
FT                   /note="Extracellular subtilisin-like protease"
FT                   /id="PRO_0000027002"
FT   DOMAIN          141..468
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   DOMAIN          484..595
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01173"
FT   ACT_SITE        171
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        237
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        409
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   595 AA;  64137 MW;  744EF9B53187442E CRC64;
     MKQSGINGVK TLTLVVCAAL ASQAYAAVNY ESANYIGSQP EGSVRFIIKY KDKSQSQQMM
     TNRSTTSVMN NNNITIAGFN AQFVRTMTIG AGIFAVPDLK TTKEAHLVMD TIASNPDVEY
     VEVDRWLRPF AAPNDPFYND QWHYYSEYGV KADKVWDRGI TGKGVTVAVV DTGIVNHPDL
     NANVIPGSGY DFIQEAEIAQ DGDGRDSNPA DAGDWHSNWA CGKYPDPRYE KRNSSWHGSH
     VAGTIAAVTN NRIGVSGVAY DAKIVPVRVL GRCGGYNSDI NEGMYWAAGG HIDGVPDNKH
     PAQVINMSLG GPGVCGSTEQ TLINRATQLG ATIIVAAGND NIDAYGVTPA SCDNILTVGA
     TTSNGTRAYF SNHGSVVDIS APGAGITSTV DSGARYPSGP SYSLMDGTSM ATPHVAGVAA
     LVISAANSVN KEMTPAQVRD VLVRTVSSFN GTPDRRIGAG IVDADAAVNA VLDGNVVERP
     IDELKPQAEY RNPQIKLIRD YQMMFSEIKV NGRPGNTKFA VVKADIRHTD PSQLKLRLVS
     PKGYEYAVHY DNIKNKSSEL ITFPRDEQMN GYWRLKIVDT KRGVTGYTRG WSVAF
 
 
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