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SSI5_STRFR
ID   SSI5_STRFR              Reviewed;         107 AA.
AC   Q9R643; Q9R5B6;
DT   24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Subtilisin inhibitor-like protein 5;
DE            Short=SIL-5;
DE            Short=SIL5;
OS   Streptomyces fradiae (Streptomyces roseoflavus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1906;
RN   [1]
RP   PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC   STRAIN=Y059;
RX   PubMed=8597568; DOI=10.1016/0167-4838(95)00207-3;
RA   Terabe M., Kojima S., Taguchi S., Momose H., Miura K.;
RT   "New subtilisin-trypsin inhibitors produced by Streptomyces: primary
RT   structures and their relationship to other proteinase inhibitors from
RT   Streptomyces.";
RL   Biochim. Biophys. Acta 1292:233-240(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-31.
RX   PubMed=7763545; DOI=10.1271/bbb.57.522;
RA   Taguchi S., Kikuchi H., Kojima S., Kumagai I., Nakase T., Miura K.,
RA   Momose H.;
RT   "High frequency of SSI-like protease inhibitors among Streptomyces.";
RL   Biosci. Biotechnol. Biochem. 57:522-524(1993).
CC   -!- FUNCTION: Strong inhibitory activity toward subtilisin BPN' and, to a
CC       lesser extent, toward trypsin.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I16 (SSI) family.
CC       {ECO:0000305}.
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DR   PIR; PC1269; PC1269.
DR   PIR; S65718; S65718.
DR   AlphaFoldDB; Q9R643; -.
DR   SMR; Q9R643; -.
DR   MEROPS; I16.010; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.350.10; -; 1.
DR   HAMAP; MF_00778; SSI; 1.
DR   InterPro; IPR000691; Prot_inh_I16_SSI.
DR   InterPro; IPR020054; Prot_inh_SSI_I16_CS.
DR   InterPro; IPR023549; Subtilisin_inhibitor.
DR   InterPro; IPR036819; Subtilisin_inhibitor-like_sf.
DR   Pfam; PF00720; SSI; 1.
DR   PRINTS; PR00294; SSBTLNINHBTR.
DR   SUPFAM; SSF55399; SSF55399; 1.
DR   PROSITE; PS00999; SSI; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor; Secreted;
KW   Serine protease inhibitor.
FT   CHAIN           1..107
FT                   /note="Subtilisin inhibitor-like protein 5"
FT                   /id="PRO_0000208661"
FT   SITE            67..68
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   DISULFID        29..44
FT                   /evidence="ECO:0000250"
FT   DISULFID        65..95
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   107 AA;  11371 MW;  BCDF2F00CD56496A CRC64;
     HAPNALVLTV AKGETARTAT PLRAVTLTCA PTPGGTHPAP EAACAELRAV DGRFSALRGD
     QDRACIKIYD PLVVTAEGVW EGQRVRYERT FGNSCTLQTE AGPVFSF
 
 
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