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P00780

- SUBT_BACLI

UniProt

P00780 - SUBT_BACLI

Protein

Subtilisin Carlsberg

Gene

apr

Organism
Bacillus licheniformis
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      Previous versions | rss
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    Functioni

    Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.

    Catalytic activityi

    Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.

    Cofactori

    Binds 2 calcium ions per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi107 – 1071Calcium 1
    Active sitei137 – 1371By similarity
    Metal bindingi146 – 1461Calcium 1
    Active sitei168 – 1681By similarity
    Metal bindingi179 – 1791Calcium 1; via carbonyl oxygen
    Metal bindingi181 – 1811Calcium 1
    Metal bindingi185 – 1851Calcium 1; via carbonyl oxygen
    Metal bindingi273 – 2731Calcium 2; via carbonyl oxygen
    Metal bindingi275 – 2751Calcium 2; via carbonyl oxygen
    Metal bindingi278 – 2781Calcium 2; via carbonyl oxygen
    Active sitei325 – 3251By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. serine-type endopeptidase activity Source: InterPro

    GO - Biological processi

    1. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Sporulation

    Keywords - Ligandi

    Calcium, Metal-binding

    Protein family/group databases

    MEROPSiI09.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Subtilisin Carlsberg (EC:3.4.21.62)
    Gene namesi
    Name:apr
    OrganismiBacillus licheniformis
    Taxonomic identifieri1402 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Biotechnological usei

    Used as a detergent protease. Sold under the name Alcalase by Novozymes.

    Protein family/group databases

    Allergomei8254. Bac li Subtilisin.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929By similarityAdd
    BLAST
    Propeptidei30 – 105761 PublicationPRO_0000027179Add
    BLAST
    Chaini106 – 379274Subtilisin CarlsbergPRO_0000027180Add
    BLAST

    Keywords - PTMi

    Zymogen

    Interactioni

    Protein-protein interaction databases

    IntActiP00780. 2 interactions.
    MINTiMINT-1505000.

    Structurei

    Secondary structure

    1
    379
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi112 – 1154
    Helixi118 – 1236
    Beta strandi132 – 1387
    Beta strandi149 – 1546
    Beta strandi156 – 1583
    Beta strandi161 – 1633
    Beta strandi165 – 1673
    Helixi168 – 17710
    Beta strandi180 – 1845
    Beta strandi192 – 1987
    Beta strandi204 – 2063
    Helixi208 – 22013
    Beta strandi224 – 2285
    Beta strandi230 – 2345
    Helixi237 – 24812
    Beta strandi252 – 2565
    Turni272 – 2743
    Beta strandi278 – 2847
    Beta strandi300 – 3056
    Beta strandi307 – 3137
    Turni314 – 3163
    Beta strandi317 – 3215
    Helixi324 – 34118
    Helixi347 – 35610
    Helixi364 – 3674
    Helixi374 – 3774

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AF4X-ray2.60A106-379[»]
    1AV7X-ray2.60A106-379[»]
    1AVTX-ray2.00A106-379[»]
    1BE6X-ray2.15A106-379[»]
    1BE8X-ray2.20A106-379[»]
    1BFKX-ray2.30A106-379[»]
    1BFUX-ray2.20A106-379[»]
    1C3LX-ray2.16A106-378[»]
    1CSEX-ray1.20E106-379[»]
    1OYVX-ray2.50A/B106-379[»]
    1R0RX-ray1.10E106-378[»]
    1SBCX-ray2.50A106-379[»]
    1SCAX-ray2.00A106-379[»]
    1SCBX-ray2.30A106-379[»]
    1SCDX-ray2.30A106-379[»]
    1SCNX-ray1.90E106-379[»]
    1SELX-ray2.00A/B106-379[»]
    1VSBX-ray2.10A106-379[»]
    1YU6X-ray1.55A/B106-379[»]
    2SECX-ray1.80E106-379[»]
    2WUVX-ray2.24A106-379[»]
    2WUWX-ray2.23E106-379[»]
    3UNXX-ray1.26A106-379[»]
    3VSBX-ray2.60A106-379[»]
    ProteinModelPortaliP00780.
    SMRiP00780. Positions 37-104, 106-379.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00780.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini132 – 377246Peptidase S8Add
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S8 family.Curated
    Contains 1 peptidase S8 domain.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.40.50.200. 1 hit.
    InterProiIPR010259. Inhibitor_I9.
    IPR000209. Peptidase_S8/S53_dom.
    IPR023827. Peptidase_S8_Asp-AS.
    IPR022398. Peptidase_S8_His-AS.
    IPR023828. Peptidase_S8_Ser-AS.
    IPR015500. Peptidase_S8_subtilisin-rel.
    IPR009020. Prot_inh_propept.
    [Graphical view]
    PANTHERiPTHR10795. PTHR10795. 1 hit.
    PfamiPF05922. Inhibitor_I9. 1 hit.
    PF00082. Peptidase_S8. 1 hit.
    [Graphical view]
    PRINTSiPR00723. SUBTILISIN.
    SUPFAMiSSF52743. SSF52743. 1 hit.
    SSF54897. SSF54897. 1 hit.
    PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
    PS00137. SUBTILASE_HIS. 1 hit.
    PS00138. SUBTILASE_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P00780-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMRKKSFWLG MLTAFMLVFT MAFSDSASAA QPAKNVEKDY IVGFKSGVKT    50
    ASVKKDIIKE SGGKVDKQFR IINAAKAKLD KEALKEVKND PDVAYVEEDH 100
    VAHALAQTVP YGIPLIKADK VQAQGFKGAN VKVAVLDTGI QASHPDLNVV 150
    GGASFVAGEA YNTDGNGHGT HVAGTVAALD NTTGVLGVAP SVSLYAVKVL 200
    NSSGSGTYSG IVSGIEWATT NGMDVINMSL GGPSGSTAMK QAVDNAYARG 250
    VVVVAAAGNS GSSGNTNTIG YPAKYDSVIA VGAVDSNSNR ASFSSVGAEL 300
    EVMAPGAGVY STYPTSTYAT LNGTSMASPH VAGAAALILS KHPNLSASQV 350
    RNRLSSTATY LGSSFYYGKG LINVEAAAQ 379
    Length:379
    Mass (Da):38,908
    Last modified:August 1, 1988 - v1
    Checksum:iF19A6DC5761FB504
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti207 – 2071T → S AA sequence (PubMed:4967581)Curated
    Sequence conflicti233 – 2331P → A AA sequence (PubMed:4967581)Curated
    Sequence conflicti262 – 2654SSGN → NSGS AA sequence (PubMed:4967581)Curated
    Sequence conflicti316 – 3161S → N AA sequence (PubMed:4967581)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03341 Genomic DNA. Translation: CAB56500.1.
    PIRiA24111. SUBSCL.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03341 Genomic DNA. Translation: CAB56500.1 .
    PIRi A24111. SUBSCL.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AF4 X-ray 2.60 A 106-379 [» ]
    1AV7 X-ray 2.60 A 106-379 [» ]
    1AVT X-ray 2.00 A 106-379 [» ]
    1BE6 X-ray 2.15 A 106-379 [» ]
    1BE8 X-ray 2.20 A 106-379 [» ]
    1BFK X-ray 2.30 A 106-379 [» ]
    1BFU X-ray 2.20 A 106-379 [» ]
    1C3L X-ray 2.16 A 106-378 [» ]
    1CSE X-ray 1.20 E 106-379 [» ]
    1OYV X-ray 2.50 A/B 106-379 [» ]
    1R0R X-ray 1.10 E 106-378 [» ]
    1SBC X-ray 2.50 A 106-379 [» ]
    1SCA X-ray 2.00 A 106-379 [» ]
    1SCB X-ray 2.30 A 106-379 [» ]
    1SCD X-ray 2.30 A 106-379 [» ]
    1SCN X-ray 1.90 E 106-379 [» ]
    1SEL X-ray 2.00 A/B 106-379 [» ]
    1VSB X-ray 2.10 A 106-379 [» ]
    1YU6 X-ray 1.55 A/B 106-379 [» ]
    2SEC X-ray 1.80 E 106-379 [» ]
    2WUV X-ray 2.24 A 106-379 [» ]
    2WUW X-ray 2.23 E 106-379 [» ]
    3UNX X-ray 1.26 A 106-379 [» ]
    3VSB X-ray 2.60 A 106-379 [» ]
    ProteinModelPortali P00780.
    SMRi P00780. Positions 37-104, 106-379.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P00780. 2 interactions.
    MINTi MINT-1505000.

    Chemistry

    BindingDBi P00780.
    ChEMBLi CHEMBL4299.

    Protein family/group databases

    Allergomei 8254. Bac li Subtilisin.
    MEROPSi I09.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P00780.

    Family and domain databases

    Gene3Di 3.40.50.200. 1 hit.
    InterProi IPR010259. Inhibitor_I9.
    IPR000209. Peptidase_S8/S53_dom.
    IPR023827. Peptidase_S8_Asp-AS.
    IPR022398. Peptidase_S8_His-AS.
    IPR023828. Peptidase_S8_Ser-AS.
    IPR015500. Peptidase_S8_subtilisin-rel.
    IPR009020. Prot_inh_propept.
    [Graphical view ]
    PANTHERi PTHR10795. PTHR10795. 1 hit.
    Pfami PF05922. Inhibitor_I9. 1 hit.
    PF00082. Peptidase_S8. 1 hit.
    [Graphical view ]
    PRINTSi PR00723. SUBTILISIN.
    SUPFAMi SSF52743. SSF52743. 1 hit.
    SSF54897. SSF54897. 1 hit.
    PROSITEi PS00136. SUBTILASE_ASP. 1 hit.
    PS00137. SUBTILASE_HIS. 1 hit.
    PS00138. SUBTILASE_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, sequencing and expression of subtilisin Carlsberg from Bacillus licheniformis."
      Jacobs M., Eliasson M., Uhlen M., Flock J.-I.
      Nucleic Acids Res. 13:8913-8926(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: NCIMB 6816 / CCM 2182 / NCDO 727.
    2. "Subtilisin Carlsberg. V. The complete sequence; comparison with subtilisin BPN'; evolutionary relationships."
      Smith E.L., Delange R.J., Evans W.H., Landon M., Markland F.S.
      J. Biol. Chem. 243:2184-2191(1968) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 106-379.
    3. "Crystal structure of selenosubtilisin at 2.0-A resolution."
      Syed R., Wu Z.P., Hogle J.M., Hilvert D.
      Biochemistry 32:6157-6164(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT WITH SELENOCYSTEINE-325.
    4. "Differences in binding modes of enantiomers of 1-acetamido boronic acid based protease inhibitors: crystal structures of gamma-chymotrypsin and subtilisin Carlsberg complexes."
      Stoll V.S., Eger B.T., Hynes R.C., Martichonok V., Jones J.B., Pai E.F.
      Biochemistry 37:451-462(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 106-379.

    Entry informationi

    Entry nameiSUBT_BACLI
    AccessioniPrimary (citable) accession number: P00780
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Secretion of subtilisin is associated with onset of sporulation, and many mutations which block sporulation at early stages affect expression levels of subtilisin. However, subtilisin is not necessary for normal sporulation.

    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