ID   SPI_BRECH               Reviewed;         326 AA.
AC   P43131;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Protease inhibitor;
DE   AltName: Full=BBRPI;
DE   Contains:
DE     RecName: Full=Serine protease inhibitor;
DE   Contains:
DE     RecName: Full=Serine protease inhibitor C;
DE   Contains:
DE     RecName: Full=Serine protease inhibitor B;
DE   Contains:
DE     RecName: Full=Serine protease inhibitor A;
DE   Flags: Precursor;
OS   Brevibacillus choshinensis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=54911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 25-32; 104-112
RP   AND 122-136.
RC   STRAIN=HPD31;
RX   PubMed=1610177; DOI=10.1128/aem.58.2.525-531.1992;
RA   Shiga Y., Hasegawa K., Tsuboi A., Yamagata H., Udaka S.;
RT   "Characterization of an extracellular protease inhibitor of Bacillus brevis
RT   HPD31 and nucleotide sequence of the corresponding gene.";
RL   Appl. Environ. Microbiol. 58:525-531(1992).
CC   -!- FUNCTION: Shows inhibitory activity towards serine proteases, such as
CC       trypsin, chymotrypsin and subtilisin. May form a trypsin-inhibitor
CC       complex in a molar ratio of 1:1.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermostable at neutral and acidic pHs.;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: Proteolytically cleaved to yield at least three forms (BBRPI-A,
CC       -B, and -C).
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DR   EMBL; D10696; BAA01538.1; -; Genomic_DNA.
DR   AlphaFoldDB; P43131; -.
DR   SMR; P43131; -.
DR   STRING; 54911.AN963_29200; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.457.10; -; 1.
DR   InterPro; IPR012854; Cu_amine_oxidase-like_N.
DR   InterPro; IPR036582; Mao_N_sf.
DR   Pfam; PF07833; Cu_amine_oxidN1; 1.
DR   SUPFAM; SSF55383; SSF55383; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Protease inhibitor; Repeat; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:1610177"
FT   CHAIN           25..326
FT                   /note="Serine protease inhibitor"
FT                   /id="PRO_0000022398"
FT   CHAIN           104..326
FT                   /note="Serine protease inhibitor C"
FT                   /id="PRO_0000022399"
FT   CHAIN           104..?
FT                   /note="Serine protease inhibitor B"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000022400"
FT   CHAIN           122..326
FT                   /note="Serine protease inhibitor A"
FT                   /id="PRO_0000022401"
FT   REPEAT          177..208
FT                   /note="1"
FT   REPEAT          272..304
FT                   /note="2"
FT   REGION          177..304
FT                   /note="2 X 32 AA approximate repeats"
SQ   SEQUENCE   326 AA;  35100 MW;  1C0456ABFA912F77 CRC64;
     MKTIRTGMMT LAALAVLGTN VVSATSEPVK ELSVNVNGQH IEQAAIFDKG QQTVLVPLRD
     VAESLGFQVK WNAETKAAEV NKGAIFSYAK VGEDRYPFAK MYKTLGAEPR LLNGNTYVPV
     AFVDEILQAE VNVTDDAVTV VDEESDVAPV RTGTITTLNK REDGGVSFQL NGYETGIILH
     VDKETKITTA DGKELKPEDL QLGMEVEATH QKFMAMSMPQ SGAVSIVVKS GLETPEVLGT
     AGKVASIDKD QEGSYKMLVE GQALAENAPE KVALIVGKDT KIVSAKDNKE LAPEDLKAEM
     KVFAYYGPKL TRSLPPIGVA EKIVVE