ID   IBB_PHAAT               Reviewed;          80 AA.
AC   P83311;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Bowman-Birk type proteinase inhibitor;
DE   AltName: Full=TBPI-B;
OS   Phaseolus acutifolius (Tepary bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX   NCBI_TaxID=33129;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, SUBUNIT, CALCIUM-BINDING, AND MASS SPECTROMETRY.
RC   TISSUE=Seed {ECO:0000269|PubMed:15051044};
RX   PubMed=15051044; DOI=10.1016/j.plaphy.2003.12.002;
RA   Campos J.E., Whitaker J.R., Yip T.-T., Hutchens T.W., Blanco-Labra A.;
RT   "Unusual structural characteristics and complete amino acid sequence of a
RT   protease inhibitor from Phaseolus acutifolius seeds.";
RL   Plant Physiol. Biochem. 42:209-214(2004).
RN   [2] {ECO:0000305}
RP   FUNCTION, AND STABILITY.
RC   TISSUE=Seed {ECO:0000269|Ref.2};
RX   AGRICOLA=IND21635738; DOI=10.1111/j.1745-4514.1997.tb00215.x;
RA   Campos J.E., Martinez-Gallardo N., Mendiola-Olaya E., Blanco-Labra A.;
RT   "Purification and partial characterization of a proteinase inhibitor from
RT   tepary bean (Phaseolus acutifolius) seeds.";
RL   J. Food Biochem. 21:203-218(1997).
CC   -!- FUNCTION: Protease inhibitor with activity against cysteine, aspartic
CC       and serine proteases. Highest activity against serine proteases, in
CC       particular trypsin and trypsin-like proteases. {ECO:0000269|Ref.2}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Stable at acidic pHs. Inhibitory activity is unaffected after 1 hour
CC         at pH 3.0 and 96 degrees Celsius. Inactivated after 1 hour at pH 10.7
CC         and 96 degrees Celsius.;
CC   -!- SUBUNIT: Occurs as a monomer, dimer or trimer. The dimer may be the
CC       active form. {ECO:0000269|PubMed:15051044}.
CC   -!- PTM: Binds calcium, probably through His-3 to His-6.
CC       {ECO:0000269|PubMed:15051044, ECO:0000303|PubMed:15051044}.
CC   -!- MASS SPECTROMETRY: Mass=9159; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15051044};
CC   -!- MASS SPECTROMETRY: Mass=9158; Method=SELDI;
CC       Evidence={ECO:0000269|PubMed:15051044};
CC   -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC       family. {ECO:0000255}.
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DR   AlphaFoldDB; P83311; -.
DR   SMR; P83311; -.
DR   MEROPS; I12.001; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   CDD; cd00023; BBI; 1.
DR   Gene3D; 2.10.69.10; -; 1.
DR   InterPro; IPR035995; Bowman-Birk_prot_inh.
DR   InterPro; IPR000877; Prot_inh_BBI.
DR   Pfam; PF00228; Bowman-Birk_leg; 1.
DR   SMART; SM00269; BowB; 1.
DR   SUPFAM; SSF57247; SSF57247; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW   Serine protease inhibitor.
FT   CHAIN           1..80
FT                   /note="Bowman-Birk type proteinase inhibitor"
FT                   /id="PRO_0000105848"
FT   SITE            27..28
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250|UniProtKB:P01055"
FT   SITE            51..52
FT                   /note="Reactive bond for chymotrypsin"
FT                   /evidence="ECO:0000250|UniProtKB:P01055"
FT   DISULFID        19..70
FT                   /evidence="ECO:0000250|UniProtKB:P01055"
FT   DISULFID        20..35
FT                   /evidence="ECO:0000250|UniProtKB:P01055"
FT   DISULFID        23..66
FT                   /evidence="ECO:0000250|UniProtKB:P01055"
FT   DISULFID        25..33
FT                   /evidence="ECO:0000250|UniProtKB:P01055"
FT   DISULFID        41..47
FT                   /evidence="ECO:0000250|UniProtKB:P01055"
FT   DISULFID        44..59
FT                   /evidence="ECO:0000250|UniProtKB:P01055"
FT   DISULFID        49..57
FT                   /evidence="ECO:0000250|UniProtKB:P01055"
SQ   SEQUENCE   80 AA;  8723 MW;  AC5D32CA2463C728 CRC64;
     SGHHHHDSSD EPSESSKACC DHCACTKSIP PQCRCALRLN CNHCRSCICT FSIPAQCVCT
     DTNDFCYEPC KSGHDDDDSG