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Reviewed, UniProtKB/Swiss-Prot P00776 (PRTA_STRGR)

Last modified June 16, 2009. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Streptogrisin-A
    EC=3.4.21.80
Alternative name(s):
    Serine protease A
    SGPA
    Pronase enzyme A
Gene names
Name: sprA
OrganismStreptomyces griseus
Taxonomic identifier1911 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Has a primary specificity for large aliphatic or aromatic amino acids.

Catalytic activity

Hydrolysis of proteins with specificity similar to chymotrypsin.

Subunit structure

Monomer.

Sequence similarities

Belongs to the peptidase S1 family.

Ontologies

Keywords
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Zymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: InterPro

   Molecular functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3838
Propeptide39 – 11577 Ref.2
PRO_0000026909
Chain116 – 297182Streptogrisin-A
PRO_0000026910

Sites

Active site1491Charge relay system By similarity
Active site1711Charge relay system By similarity
Active site2531Charge relay system By similarity

Amino acid modifications

Disulfide bond130 ↔ 150 Ref.5
Disulfide bond247 ↔ 274 Ref.5

Experimental info

Sequence conflict1511T → TS AA sequence Ref.2
Sequence conflict1841D → N AA sequence Ref.2

Secondary structure

.......................................... 297
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00776-1 [UniParc].

Last modified February 1, 1991. Version 2.
Checksum: 7F6CF04A81B4B3C9

FASTA29729,663
        10         20         30         40         50         60 
MTFKRFSPLS STSRYARLLA VASGLVAAAA LATPSAVAAP EAESKATVSQ LADASSAILA 

        70         80         90        100        110        120 
ADVAGTAWYT EASTGKIVLT ADSTVSKAEL AKVSNALAGS KAKLTVKRAE GKFTPLIAGG 

       130        140        150        160        170        180 
EAITTGGSRC SLGFNVSVNG VAHALTAGHC TNISASWSIG TRTGTSFPNN DYGIIRHSNP 

       190        200        210        220        230        240 
AAADGRVYLY NGSYQDITTA GNAFVGQAVQ RSGSTTGLRS GSVTGLNATV NYGSSGIVYG 

       250        260        270        280        290 
MIQTNVCAEP GDSGGSLFAG STALGLTSGG SGNCRTGGTT FYQPVTEALS AYGATVL 

« Hide

References

[1]"Characterization and structure of genes for proteases A and B from Streptomyces griseus."
Henderson G., Krygsman P., Liu C.J., Davey C.C., Malek L.T.
J. Bacteriol. 169:3778-3784(1987) [PubMed: 3112129] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The amino acid sequence and predicted structure of Streptomyces griseus protease A."
Johnson P., Smillie L.B.
FEBS Lett. 47:1-6(1974) [PubMed: 4214713] [Abstract]
Cited for: PROTEIN SEQUENCE OF 116-297.
[3]Apostol I., Smillie L.B., Laskowski M. Jr.
Submitted (JUL-1996) to UniProtKB
Cited for: SEQUENCE REVISION TO 249.
[4]"Protein structure refinement: Streptomyces griseus serine protease A at 1.8-A resolution."
Sielecki A.R., Hendrickson W.A., Broughton C.G., Delbaere L.T.J., Brayer G.D., James M.N.G.
J. Mol. Biol. 134:781-804(1979) [PubMed: 119870] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[5]"Molecular structure of crystalline Streptomyces griseus protease A at 2.8-A resolution. II. Molecular conformation, comparison with alpha-chymotrypsin and active-site geometry."
Brayer G.D., Delbaere L.T.J., James M.N.G.
J. Mol. Biol. 124:261-283(1978) [PubMed: 101674] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

M17103 Genomic DNA. Translation: AAA26818.1.
PIRPRSMAG. A26974.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1SGCX-ray1.80A117-297[»]
2SGAX-ray1.50A117-297[»]
3SGAX-ray1.80E117-297[»]
4SGAX-ray1.80E117-297[»]
5SGAX-ray1.80E117-297[»]
ModBaseSearch...

Protein family/group databases

MEROPSS01.261.

Enzyme and pathway databases

BRENDA3.4.21.80. 1270.

Family and domain databases

InterProIPR004236. Pept_S1_alpha_lytic.
IPR001316. Pept_S1A_streptogrisin.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
[Graphical view]
PfamPF02983. Pro_Al_protease. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001134. Streptogrisin. 1 hit.
PRINTSPR00861. ALYTICPTASE.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
PROSITEPS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePRTA_STRGR
AccessionPrimary (citable) accession number: P00776
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1991
Last modified: June 16, 2009
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents