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P00777 (PRTB_STRGR) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Streptogrisin-B

EC=3.4.21.81
Alternative name(s):
Pronase enzyme B
SGPB
Serine protease B
Gene names
Name:sprB
OrganismStreptomyces griseus
Taxonomic identifier1911 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length299 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 trypsin-like specificity.

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)
   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 – 11476
PRO_0000026911
Chain115 – 299185Streptogrisin-B
PRO_0000026912

Sites

Active site1471Charge relay system Ref.6 Ref.7
Active site1771Charge relay system Ref.6 Ref.7
Active site2551Charge relay system Ref.6 Ref.7

Amino acid modifications

Disulfide bond128 ↔ 148
Disulfide bond249 ↔ 276

Experimental info

Sequence conflict1531T → TG AA sequence Ref.2
Sequence conflict1571Missing AA sequence Ref.2
Sequence conflict2931A → V AA sequence Ref.2
Sequence conflict2961V → A AA sequence Ref.2

Secondary structure

...................................... 299
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00777 [UniParc].

Last modified February 1, 1991. Version 2.
Checksum: 7A272C9516C7B9B1

FASTA29930,554
        10         20         30         40         50         60 
MRIKRTSNRS NAARRVRTTA VLAGLAAVAA LAVPTANAET PRTFSANQLT AASDAVLGAD 

        70         80         90        100        110        120 
IAGTAWNIDP QSKRLVVTVD STVSKAEINQ IKKSAGANAD ALRIERTPGK FTKLISGGDA 

       130        140        150        160        170        180 
IYSSTGRCSL GFNVRSGSTY YFLTAGHCTD GATTWWANSA RTTVLGTTSG SSFPNNDYGI 

       190        200        210        220        230        240 
VRYTNTTIPK DGTVGGQDIT SAANATVGMA VTRRGSTTGT HSGSVTALNA TVNYGGGDVV 

       250        260        270        280        290 
YGMIRTNVCA EPGDSGGPLY SGTRAIGLTS GGSGNCSSGG TTFFQPVTEA LSAYGVSVY 

« 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Amino acid sequence of Streptomyces griseus protease B, A MAJOR COMPONENT OF Pronase."
Jurasek L., Carpenter M.R., Smillie L.B., Gertler A., Levy S., Ericsson L.H.
Biochem. Biophys. Res. Commun. 61:1095-1100(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 115-299.
Strain: K-1.
[3]"Tertiary structural differences between microbial serine proteases and pancreatic serine enzymes."
Delbaere L.T.J., Hutcheon W.L.B., James M.N.G., Thiessen W.E.
Nature 257:758-763(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SEQUENCE REVISION.
[4]"The 2.8-A resolution structure of Streptomyces griseus protease B and its homology with alpha-chymotrypsin and Streptomyces griseus protease A."
Delbaere L.T.J., Brayer G.D., James M.N.G.
Can. J. Biochem. 57:135-144(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SEQUENCE REVISION.
[5]"Structure of the complex of Streptomyces griseus proteinase B and polypeptide chymotrypsin inhibitor-1 from Russet Burbank potato tubers at 2.1-A resolution."
Greenblatt H.M., Ryan C.A., James M.N.G.
J. Mol. Biol. 205:201-228(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[6]"Inhibition of Streptomyces griseus protease B by peptide chloromethyl ketones: partial mapping of the binding site and identification of the reactive residue."
Gertler A.
FEBS Lett. 43:81-85(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE.
[7]"Studies on Streptomyces griseus protease. II. The amino acid sequence around the reactive serine residue of DFP-sensitive components with esterase activity."
Wahlby S., Engstrom L.
Biochim. Biophys. Acta 151:402-408(1968) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17104 Genomic DNA. Translation: AAA26819.1.
PIRPRSMBG. B26974.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CSOX-ray1.90E115-299[»]
1CT0X-ray1.80E115-299[»]
1CT2X-ray1.65E115-299[»]
1CT4X-ray1.60E115-299[»]
1DS2X-ray1.70E115-299[»]
1SGDX-ray1.80E115-299[»]
1SGEX-ray1.80E115-299[»]
1SGNX-ray1.80E115-299[»]
1SGPX-ray1.40E115-299[»]
1SGQX-ray1.90E115-299[»]
1SGRX-ray1.80E115-299[»]
1SGYX-ray1.80E115-299[»]
2GKVX-ray1.70E115-260[»]
2NU0X-ray1.95E115-299[»]
2NU1X-ray1.80E115-299[»]
2NU2X-ray1.65E115-299[»]
2NU3X-ray1.80E115-299[»]
2NU4X-ray1.75E115-299[»]
2QA9X-ray1.18E115-299[»]
I119-122[»]
2QAAX-ray1.23A/B115-299[»]
2SGDX-ray1.80E115-299[»]
2SGEX-ray1.80E115-299[»]
2SGFX-ray1.75E115-299[»]
2SGPX-ray1.80E115-299[»]
2SGQX-ray1.80E115-299[»]
3SGBX-ray1.80E115-299[»]
3SGQX-ray1.80E115-299[»]
4SGBX-ray2.10E115-299[»]
ProteinModelPortalP00777.
SMRP00777. Positions 115-299.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-1504708.

Protein family/group databases

Allergome3640. Str g Pronase.
MEROPSS01.262.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR004236. Pept_S1_alpha_lytic.
IPR001316. Pept_S1A_streptogrisin.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR009003. Trypsin-like_Pept_dom.
[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]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00777.
PMAP-CutDBP00777.

Entry information

Entry namePRTB_STRGR
AccessionPrimary (citable) accession number: P00777
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1991
Last modified: July 9, 2014
This is version 104 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

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references