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P00777

- PRTB_STRGR

UniProt

P00777 - PRTB_STRGR

Protein

Streptogrisin-B

Gene

sprB

Organism
Streptomyces griseus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (01 Feb 1991)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

    Hydrolysis of proteins with trypsin-like specificity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei147 – 1471Charge relay system
    Active sitei177 – 1771Charge relay system
    Active sitei255 – 2551Charge relay system

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Protein family/group databases

    MEROPSiS01.262.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Streptogrisin-B (EC:3.4.21.81)
    Alternative name(s):
    Pronase enzyme B
    SGPB
    Serine protease B
    Gene namesi
    Name:sprB
    OrganismiStreptomyces griseus
    Taxonomic identifieri1911 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: InterPro

    Pathology & Biotechi

    Protein family/group databases

    Allergomei3640. Str g Pronase.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3838Add
    BLAST
    Propeptidei39 – 114761 PublicationPRO_0000026911Add
    BLAST
    Chaini115 – 299185Streptogrisin-BPRO_0000026912Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi128 ↔ 148
    Disulfide bondi249 ↔ 276

    Keywords - PTMi

    Disulfide bond, Zymogen

    Miscellaneous databases

    PMAP-CutDBP00777.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    MINTiMINT-1504708.

    Structurei

    Secondary structure

    1
    299
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi120 – 1223
    Beta strandi127 – 1293
    Beta strandi132 – 1365
    Beta strandi139 – 1446
    Helixi146 – 1494
    Beta strandi153 – 1586
    Beta strandi163 – 17210
    Beta strandi174 – 1763
    Beta strandi178 – 1836
    Beta strandi186 – 1883
    Beta strandi192 – 1943
    Beta strandi210 – 2156
    Turni216 – 2183
    Beta strandi219 – 23315
    Beta strandi235 – 2373
    Beta strandi239 – 2479
    Beta strandi258 – 2614
    Beta strandi264 – 27512
    Turni276 – 2783
    Beta strandi279 – 2868
    Helixi287 – 2948

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP00777.
    SMRiP00777. Positions 115-299.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00777.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S1 family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    InterProiIPR004236. Pept_S1_alpha_lytic.
    IPR001316. Pept_S1A_streptogrisin.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF02983. Pro_Al_protease. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001134. Streptogrisin. 1 hit.
    PRINTSiPR00861. ALYTICPTASE.
    SMARTiSM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    PROSITEiPS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00777-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRIKRTSNRS NAARRVRTTA VLAGLAAVAA LAVPTANAET PRTFSANQLT    50
    AASDAVLGAD IAGTAWNIDP QSKRLVVTVD STVSKAEINQ IKKSAGANAD 100
    ALRIERTPGK FTKLISGGDA IYSSTGRCSL GFNVRSGSTY YFLTAGHCTD 150
    GATTWWANSA RTTVLGTTSG SSFPNNDYGI VRYTNTTIPK DGTVGGQDIT 200
    SAANATVGMA VTRRGSTTGT HSGSVTALNA TVNYGGGDVV YGMIRTNVCA 250
    EPGDSGGPLY SGTRAIGLTS GGSGNCSSGG TTFFQPVTEA LSAYGVSVY 299
    Length:299
    Mass (Da):30,554
    Last modified:February 1, 1991 - v2
    Checksum:i7A272C9516C7B9B1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti153 – 1531T → TG AA sequence (PubMed:4218101)Curated
    Sequence conflicti157 – 1571Missing AA sequence (PubMed:4218101)Curated
    Sequence conflicti293 – 2931A → V AA sequence (PubMed:4218101)Curated
    Sequence conflicti296 – 2961V → A AA sequence (PubMed:4218101)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17104 Genomic DNA. Translation: AAA26819.1.
    PIRiB26974. PRSMBG.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17104 Genomic DNA. Translation: AAA26819.1 .
    PIRi B26974. PRSMBG.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CSO X-ray 1.90 E 115-299 [» ]
    1CT0 X-ray 1.80 E 115-299 [» ]
    1CT2 X-ray 1.65 E 115-299 [» ]
    1CT4 X-ray 1.60 E 115-299 [» ]
    1DS2 X-ray 1.70 E 115-299 [» ]
    1SGD X-ray 1.80 E 115-299 [» ]
    1SGE X-ray 1.80 E 115-299 [» ]
    1SGN X-ray 1.80 E 115-299 [» ]
    1SGP X-ray 1.40 E 115-299 [» ]
    1SGQ X-ray 1.90 E 115-299 [» ]
    1SGR X-ray 1.80 E 115-299 [» ]
    1SGY X-ray 1.80 E 115-299 [» ]
    2GKV X-ray 1.70 E 115-260 [» ]
    2NU0 X-ray 1.95 E 115-299 [» ]
    2NU1 X-ray 1.80 E 115-299 [» ]
    2NU2 X-ray 1.65 E 115-299 [» ]
    2NU3 X-ray 1.80 E 115-299 [» ]
    2NU4 X-ray 1.75 E 115-299 [» ]
    2QA9 X-ray 1.18 E 115-299 [» ]
    I 119-122 [» ]
    2QAA X-ray 1.23 A/B 115-299 [» ]
    2SGD X-ray 1.80 E 115-299 [» ]
    2SGE X-ray 1.80 E 115-299 [» ]
    2SGF X-ray 1.75 E 115-299 [» ]
    2SGP X-ray 1.80 E 115-299 [» ]
    2SGQ X-ray 1.80 E 115-299 [» ]
    3SGB X-ray 1.80 E 115-299 [» ]
    3SGQ X-ray 1.80 E 115-299 [» ]
    4SGB X-ray 2.10 E 115-299 [» ]
    ProteinModelPortali P00777.
    SMRi P00777. Positions 115-299.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-1504708.

    Protein family/group databases

    Allergomei 3640. Str g Pronase.
    MEROPSi S01.262.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P00777.
    PMAP-CutDB P00777.

    Family and domain databases

    InterProi IPR004236. Pept_S1_alpha_lytic.
    IPR001316. Pept_S1A_streptogrisin.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF02983. Pro_Al_protease. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001134. Streptogrisin. 1 hit.
    PRINTSi PR00861. ALYTICPTASE.
    SMARTi SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    PROSITEi PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiPRTB_STRGR
    AccessioniPrimary (citable) accession number: P00777
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 105 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3