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P01006 (SSI_STRAO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Subtilisin inhibitor
Alternative name(s):
SSI type
Gene names
Name:ssi
OrganismStreptomyces albogriseolus
Taxonomic identifier1887 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length144 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Strong inhibitor of bacterial serine proteases such as subtilisin. HAMAP-Rule MF_00778

Subunit structure

Homodimer.

Subcellular location

Secreted HAMAP-Rule MF_00778.

Sequence similarities

Belongs to the protease inhibitor I16 (SSI) family. [View classification]

Ontologies

Keywords
   Cellular componentSecreted
   DomainRepeat
Signal
   Molecular functionProtease inhibitor
Serine protease inhibitor
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionserine-type endopeptidase inhibitor activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Ref.5
Chain32 – 144113Subtilisin inhibitor HAMAP-Rule MF_00778
PRO_0000033270

Regions

Repeat33 – 375 HAMAP-Rule MF_00778
Repeat39 – 435 HAMAP-Rule MF_00778

Sites

Site104 – 1052Reactive bond for subtilisin

Amino acid modifications

Disulfide bond66 ↔ 81 HAMAP-Rule MF_00778
Disulfide bond102 ↔ 132 HAMAP-Rule MF_00778

Experimental info

Mutagenesis1041M → D, E, V, I, G or P: Decrease in inhibition. Ref.9 Ref.10
Mutagenesis1041M → K or R: Also inhibits trypsin. Ref.9 Ref.10
Mutagenesis1041M → Y or W: Also inhibits chymotrypsin. Ref.9 Ref.10

Secondary structure

....................... 144
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01006 [UniParc].

Last modified November 1, 1990. Version 2.
Checksum: BEA57AC7FDCD8004

FASTA14414,312
        10         20         30         40         50         60 
MRNTGAGPSP SVSRPPPSAA PLSGAALAAP GDAPSALYAP SALVLTVGKG VSATTAAPER 

        70         80         90        100        110        120 
AVTLTCAPGP SGTHPAAGSA CADLAAVGGD LNALTRGEDV MCPMVYDPVL LTVDGVWQGK 

       130        140 
RVSYERVFSN ECEMNAHGSS VFAF 

« Hide

References

[1]"Molecular cloning and nucleotide sequence determination of gene encoding Streptomyces subtilisin inhibitor (SSI)."
Obata S., Taguchi S., Kumagai I., Miura K.
J. Biochem. 105:367-371(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: S-3253.
[2]"Partial alteration of a protein Streptomyces subtilisin inhibitor by site-directed mutagenesis."
Miura K., Kumagai I., Obata S., Kojima S., Taguchi S.
Proc. Jpn. Acad., B, Phys. Biol. Sci. 64:147-149(1988)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Analysis of transcriptional control regions in the Streptomyces subtilisin-inhibitor-encoding gene."
Taguchi S., Nishiyama K., Kumagai I., Miura K.
Gene 84:279-286(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-144.
Strain: S-3253.
[4]"Effect of a rare leucine codon, TTA, on expression of a foreign gene in Streptomyces lividans."
Ueda Y., Taguchi S., Nishiyama K., Kumagai I., Miura K.
Biochim. Biophys. Acta 1172:262-266(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-144.
[5]"Amino acid sequence of an alkaline proteinase inhibitor (Streptomyces subtilisin inhibitor) from Streptomyces albogriseolus S-3253."
Ikenaka T., Odani S., Sakai M., Nabeshima Y., Sato S., Murao S.
J. Biochem. 76:1191-1209(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 32-144.
Strain: S-3253.
[6]"Importance of the carboxyl-terminal four amino acid residues in the inhibitory activity of Streptomyces subtilisin inhibitor (with a revision of its carboxyl-terminal sequence)."
Sakai M., Odani S., Ikenaka T.
J. Biochem. 87:891-898(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 142-143.
[7]"Crystal structures of Streptomyces subtilisin inhibitor and its complex with subtilisin BPN'."
Mitsui Y., Satow Y., Watanabe Y., Hirono S., Iitaka Y.
Nature 277:447-452(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[8]"Crystal structure at 2.6-A resolution of the complex of subtilisin BPN' with streptomyces subtilisin inhibitor."
Hirono S., Akagawa H., Mitsui Y., Iitaka Y.
J. Mol. Biol. 178:389-413(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[9]"Alteration of the specificity of the Streptomyces subtilisin inhibitor by gene engineering."
Kojima S., Obata S., Kumagai I., Miura K.
Biotechnology (N.Y.) 8:449-452(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF MET-104.
[10]"Inhibition of subtilisin BPN' by reaction site P1 mutants of Streptomyces subtilisin inhibitor."
Kojima S., Nishiyama Y., Kumagai I., Miura K.
J. Biochem. 109:377-382(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF MET-104.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00402 Genomic DNA. Translation: BAA00305.1.
M33133 Genomic DNA. Translation: AAA26821.1.
M33134 Genomic DNA. Translation: AAA26822.1.
X73049 Genomic DNA. Translation: CAA51525.1.
M54887 Genomic DNA. Translation: AAA26827.1.
PIRXSSMA. JX0066.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2SICX-ray1.80I38-144[»]
2TLDX-ray2.60I35-144[»]
3SICX-ray1.80I38-144[»]
3SSIX-ray2.30A32-144[»]
5SICX-ray2.20I38-144[»]
ProteinModelPortalP01006.
SMRP01006. Positions 37-144.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-1345749.

Protein family/group databases

MEROPSI16.003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.30.350.10. 1 hit.
HAMAPMF_00778. SSI.
InterProIPR000691. Prot_inh_I16_SSI.
IPR020054. Prot_inh_SSI_I16_CS.
IPR023549. Subtilisin_inhibitor.
[Graphical view]
PfamPF00720. SSI. 1 hit.
[Graphical view]
PRINTSPR00294. SSBTLNINHBTR.
ProDomPD004028. Prot_inh_SSI. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF55399. SSF55399. 1 hit.
PROSITEPS00999. SSI. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP01006.

Entry information

Entry nameSSI_STRAO
AccessionPrimary (citable) accession number: P01006
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1990
Last modified: April 16, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references