ID   PAPI_STRMB              Reviewed;         143 AA.
AC   P86242; N1NV49;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2013, sequence version 2.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Papain inhibitor {ECO:0000303|PubMed:21715969};
DE            Short=SPI {ECO:0000303|PubMed:21715969};
DE   Flags: Precursor;
GN   Name=pi;
OS   Streptomyces mobaraensis (Streptoverticillium mobaraense).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=35621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29032 / CBS 199.75 / DSM 40847 / NBRC 13819 / NCIMB 11159 /
RC   NRRL B-3729 / VKM Ac-928;
RA   Zindel S., Froels S., Kletzin A., Dehm D., Ehret V., Ehret M., Pfeifer F.,
RA   Fuchsbauer H.L.;
RT   "Gene structure of the papain inhibitor from Streptomyces mobaraensis.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 34-53, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   SUBUNIT, SUBCELLULAR LOCATION, AND INDUCTION.
RC   STRAIN=ATCC 29032 / CBS 199.75 / DSM 40847 / NBRC 13819 / NCIMB 11159 /
RC   NRRL B-3729 / VKM Ac-928 {ECO:0000269|PubMed:21715969};
RX   PubMed=21715969;
RA   Sarafeddinov A., Arif A., Peters A., Fuchsbauer H.L.;
RT   "A novel transglutaminase substrate from Streptomyces mobaraensis
RT   inhibiting papain-like cysteine proteases.";
RL   J. Microbiol. Biotechnol. 21:617-626(2011).
CC   -!- FUNCTION: Stress protein produced under hyperthermal stress conditions.
CC       Serves as a glutamine and lysine donor substrate for transglutaminase.
CC       Inhibits the cysteine proteases papain and bromelain as well as the
CC       bovine serine protease trypsin. Has hardly any or no effect on
CC       subtilisin, bovine chymotrypsin, proteinase K from T.album,
CC       transglutaminase-activating metalloproteinase (TAMEP) from
CC       S.mobaraensis, dispase from B.polymyxa, thermolysin from
CC       B.thermoproteolyticus or collagenase from C.histolyticum.
CC       {ECO:0000269|PubMed:21715969}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermostable. Activity is stable between 20-40 degrees Celsius.
CC         Retains about 70% activity after 60 min at 100 degrees Celsius.
CC         {ECO:0000269|PubMed:21715969};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:21715969}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21715969}.
CC   -!- INDUCTION: By heat stress. {ECO:0000269|PubMed:21715969}.
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DR   EMBL; HF968450; CCW72532.1; -; Genomic_DNA.
DR   PDB; 5NTB; X-ray; 1.50 A; A/B=34-143.
DR   PDB; 6GMG; X-ray; 2.25 A; C/D=34-42.
DR   PDBsum; 5NTB; -.
DR   PDBsum; 6GMG; -.
DR   AlphaFoldDB; P86242; -.
DR   SMR; P86242; -.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0010466; P:negative regulation of peptidase activity; IDA:UniProtKB.
DR   Gene3D; 2.40.40.10; -; 1.
DR   InterPro; IPR009009; RlpA-like_DPBB.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   Pfam; PF03330; DPBB_1; 1.
DR   SUPFAM; SSF50685; SSF50685; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Protease inhibitor; Secreted;
KW   Serine protease inhibitor; Signal; Thiol protease inhibitor.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000269|PubMed:21715969"
FT   CHAIN           34..143
FT                   /note="Papain inhibitor"
FT                   /id="PRO_0000413032"
FT   STRAND          41..48
FT                   /evidence="ECO:0007829|PDB:5NTB"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:5NTB"
FT   STRAND          57..61
FT                   /evidence="ECO:0007829|PDB:5NTB"
FT   TURN            62..64
FT                   /evidence="ECO:0007829|PDB:5NTB"
FT   STRAND          68..71
FT                   /evidence="ECO:0007829|PDB:5NTB"
FT   HELIX           72..74
FT                   /evidence="ECO:0007829|PDB:5NTB"
FT   STRAND          77..79
FT                   /evidence="ECO:0007829|PDB:5NTB"
FT   HELIX           80..82
FT                   /evidence="ECO:0007829|PDB:5NTB"
FT   HELIX           84..86
FT                   /evidence="ECO:0007829|PDB:5NTB"
FT   STRAND          90..95
FT                   /evidence="ECO:0007829|PDB:5NTB"
FT   STRAND          98..108
FT                   /evidence="ECO:0007829|PDB:5NTB"
FT   STRAND          115..119
FT                   /evidence="ECO:0007829|PDB:5NTB"
FT   HELIX           120..123
FT                   /evidence="ECO:0007829|PDB:5NTB"
FT   TURN            124..126
FT                   /evidence="ECO:0007829|PDB:5NTB"
FT   HELIX           129..131
FT                   /evidence="ECO:0007829|PDB:5NTB"
FT   STRAND          134..142
FT                   /evidence="ECO:0007829|PDB:5NTB"
SQ   SEQUENCE   143 AA;  15471 MW;  A299005012006279 CRC64;
     MREFRRVRRV RFAACALVAA ATGITLAAGP ASADIPIGQK MTGKMTYYTD KGYGACGTPI
     DASSQDLVAI PAAWWTTPNP NNDPLCRGVS VEVSYNGRTI RVPVRDKCPS CDRTHIDLSQ
     AAFAKLAPLD RGVVNGITWK FVR