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