ID   BSP_BOSSE               Reviewed;          64 AA.
AC   C0HJG8;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=Basic secretory protease {ECO:0000303|PubMed:22773449};
DE            EC=3.4.24.- {ECO:0000269|PubMed:22773449};
DE   AltName: Full=Boswellia basic secretory protease {ECO:0000303|PubMed:22773449};
DE            Short=BBSP {ECO:0000303|PubMed:22773449};
DE   Flags: Fragments;
OS   Boswellia serrata (Indian frankincense).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Burseraceae; Boswellia.
OX   NCBI_TaxID=613112;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, COFACTOR, ACTIVITY REGULATION, AND
RP   GLYCOSYLATION.
RC   TISSUE=Resin {ECO:0000269|PubMed:22773449};
RX   PubMed=22773449; DOI=10.1093/glycob/cws107;
RA   Herrmann A., Konig S., Lechtenberg M., Sehlbach M., Vakhrushev S.Y.,
RA   Peter-Katalinic J., Hensel A.;
RT   "Proteoglycans from Boswellia serrata Roxb. and B. carteri Birdw. and
RT   identification of a proteolytic plant basic secretory protein.";
RL   Glycobiology 22:1424-1439(2012).
CC   -!- FUNCTION: Metalloprotease, digests gelatin and azocasein (in vitro).
CC       {ECO:0000269|PubMed:22773449}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000269|PubMed:22773449};
CC   -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:22773449}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:22773449}.
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DR   AlphaFoldDB; C0HJG8; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR007541; Uncharacterised_BSP.
DR   Pfam; PF04450; BSP; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease.
FT   CHAIN           <1..>64
FT                   /note="Basic secretory protease"
FT                   /id="PRO_0000425701"
FT   NON_CONS        5..6
FT                   /evidence="ECO:0000303|PubMed:22773449"
FT   NON_CONS        8..9
FT                   /evidence="ECO:0000303|PubMed:22773449"
FT   NON_CONS        17..18
FT                   /evidence="ECO:0000303|PubMed:22773449"
FT   NON_CONS        46..47
FT                   /evidence="ECO:0000303|PubMed:22773449"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:22773449"
FT   NON_TER         64
FT                   /evidence="ECO:0000303|PubMed:22773449"
SQ   SEQUENCE   64 AA;  7324 MW;  2BB528692983D67C CRC64;
     YSLQNDPEIT LIDSTIEWDE GYDVTARFLD YLNSLDAGFV AELENKTVEQ LWSEYKASYG
     PNGQ