P01006 (SSI_STRAO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Subtilisin inhibitor

Alternative name(s):
SSI type

Gene names

Name:

ssi

Organism

Streptomyces albogriseolus

Taxonomic identifier

1887 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	144 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Secreted
Domain	Repeat Signal
Molecular function	Protease inhibitor Serine protease inhibitor
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	serine-type endopeptidase inhibitor activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 31

31

Ref.5

Chain

32 – 144

113

Subtilisin inhibitor HAMAP-Rule MF_00778

PRO_0000033270

Regions

Repeat

33 – 37

5

HAMAP-Rule MF_00778

Repeat

39 – 43

5

HAMAP-Rule MF_00778

Sites

Site

104 – 105

2

Reactive bond for subtilisin

Amino acid modifications

Disulfide bond

66 ↔ 81

HAMAP-Rule MF_00778

Disulfide bond

102 ↔ 132

HAMAP-Rule MF_00778

Experimental info

Mutagenesis

104

1

M → D, E, V, I, G or P: Decrease in inhibition. Ref.9 Ref.10

Mutagenesis

104

1

M → K or R: Also inhibits trypsin. Ref.9 Ref.10

Mutagenesis

104

1

M → Y or W: Also inhibits chymotrypsin. Ref.9 Ref.10

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

144

Helix Strand Turn

Details...

Beta strand

42 – 52

11

Turn

53 – 55

3

Beta strand

60 – 65

6

Beta strand

67 – 69

3

Beta strand

71 – 73

3

Helix

77 – 87

11

Helix

91 – 93

3

Beta strand

98 – 103

6

Beta strand

109 – 117

9

Beta strand

120 – 130

11

Helix

131 – 135

5

Beta strand

138 – 140

3

Sequences

	Sequence		Length	Mass (Da)
	P01006 [UniParc]. Last modified November 1, 1990. Version 2. Checksum: BEA57AC7FDCD8004	FASTA	144	14,312
	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

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.

PIR

XSSMA. JX0066.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2SIC	X-ray	1.80	I	38-144	[»]
2TLD	X-ray	2.60	I	35-144	[»]
3SIC	X-ray	1.80	I	38-144	[»]
3SSI	X-ray	2.30	A	32-144	[»]
5SIC	X-ray	2.20	I	38-144	[»]

ProteinModelPortal

P01006.

SMR

P01006. Positions 37-144.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-1345749.

Protein family/group databases

MEROPS

I16.003.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

3.30.350.10. 1 hit.

HAMAP

MF_00778. SSI.

InterPro

IPR000691. Prot_inh_I16_SSI.
IPR020054. Prot_inh_SSI_I16_CS.
IPR023549. Subtilisin_inhibitor.
[Graphical view]

Pfam

PF00720. SSI. 1 hit.
[Graphical view]

PRINTS

PR00294. SSBTLNINHBTR.

ProDom

PD004028. Prot_inh_SSI. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF55399. Prot_inh_SSI. 1 hit.

PROSITE

PS00999. SSI. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P01006.

Entry information

Entry name

SSI_STRAO

Accession

Primary (citable) accession number: P01006

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	November 1, 1990
Last modified:	April 3, 2013
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program