ID   IBB_PHALU               Reviewed;          83 AA.
AC   P01056;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Bowman-Birk type proteinase inhibitor;
OS   Phaseolus lunatus (Lima bean) (Phaseolus limensis).
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=3884;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Stevens F.C., Wuerz S., Krahn J.;
RT   "Structure-function relationships in lima bean protease inhibitor.";
RL   (In) Fritz H., Tschesche H., Greene L.J., Truscheit E. (eds.);
RL   Proteinase inhibitors (Bayer-symp. V), pp.344-354, Springer-Verlag, Berlin
RL   (1974).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS), AND DISULFIDE BONDS.
RX   PubMed=12554963; DOI=10.1107/s0907444902020917;
RA   Debreczeni J.E., Bunkoczi G., Girmann B., Sheldrick G.M.;
RT   "In-house phase determination of the lima bean trypsin inhibitor: a low-
RT   resolution sulfur-SAD case.";
RL   Acta Crystallogr. D 59:393-395(2003).
CC   -!- MISCELLANEOUS: Several variants were isolated from a commercial Lima
CC       bean preparation. Some lacked 8, 12, or 14 N-terminal residues and 2 C-
CC       terminal residues.
CC   -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC       family. {ECO:0000305}.
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DR   PIR; A01295; TILI.
DR   PDB; 1H34; X-ray; 2.04 A; A=1-83.
DR   PDBsum; 1H34; -.
DR   SMR; P01056; -.
DR   MEROPS; I12.001; -.
DR   MEROPS; I12.018; -.
DR   EvolutionaryTrace; P01056; -.
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; 2.
DR   SMART; SM00269; BowB; 1.
DR   SUPFAM; SSF57247; SSF57247; 1.
DR   PROSITE; PS00281; BOWMAN_BIRK; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Protease inhibitor; Serine protease inhibitor.
FT   CHAIN           1..83
FT                   /note="Bowman-Birk type proteinase inhibitor"
FT                   /id="PRO_0000105850"
FT   SITE            26..27
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   SITE            53..54
FT                   /note="Reactive bond for chymotrypsin"
FT                   /evidence="ECO:0000250"
FT   DISULFID        18..72
FT                   /evidence="ECO:0000269|PubMed:12554963,
FT                   ECO:0007744|PDB:1H34"
FT   DISULFID        19..34
FT                   /evidence="ECO:0000269|PubMed:12554963,
FT                   ECO:0007744|PDB:1H34"
FT   DISULFID        22..68
FT                   /evidence="ECO:0000269|PubMed:12554963,
FT                   ECO:0007744|PDB:1H34"
FT   DISULFID        24..32
FT                   /evidence="ECO:0000269|PubMed:12554963,
FT                   ECO:0007744|PDB:1H34"
FT   DISULFID        42..49
FT                   /evidence="ECO:0000269|PubMed:12554963,
FT                   ECO:0007744|PDB:1H34"
FT   DISULFID        46..61
FT                   /evidence="ECO:0000269|PubMed:12554963,
FT                   ECO:0007744|PDB:1H34"
FT   DISULFID        51..59
FT                   /evidence="ECO:0000269|PubMed:12554963,
FT                   ECO:0007744|PDB:1H34"
FT   VARIANT         23
FT                   /note="A -> L"
FT   VARIANT         35
FT                   /note="T -> S"
FT   VARIANT         37
FT                   /note="L -> F"
FT   VARIANT         47
FT                   /note="K -> Z"
FT   VARIANT         53
FT                   /note="L -> F"
FT   VARIANT         62
FT                   /note="B -> T"
FT   VARIANT         65
FT                   /note="B -> T"
FT   CONFLICT        23
FT                   /note="A -> S (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   STRAND          20..24
FT                   /evidence="ECO:0007829|PDB:1H34"
FT   STRAND          26..29
FT                   /evidence="ECO:0007829|PDB:1H34"
FT   STRAND          32..34
FT                   /evidence="ECO:0007829|PDB:1H34"
FT   STRAND          37..41
FT                   /evidence="ECO:0007829|PDB:1H34"
FT   STRAND          47..51
FT                   /evidence="ECO:0007829|PDB:1H34"
FT   STRAND          53..56
FT                   /evidence="ECO:0007829|PDB:1H34"
FT   STRAND          58..61
FT                   /evidence="ECO:0007829|PDB:1H34"
FT   STRAND          65..67
FT                   /evidence="ECO:0007829|PDB:1H34"
SQ   SEQUENCE   83 AA;  9079 MW;  765DEEA0253F030D CRC64;
     SGHHEHSTDZ PSZSSKPCCB HCACTKSIPP QCRCTDLRLD SCHSACKSCI CTLSIPAQCV
     CBBIBDFCYE PCKSSHSDDD NNN