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Entry version 151 (13 Nov 2019)
Sequence version 2 (18 Sep 2019)
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Protein

Subtilisin Carlsberg

Gene

subC

Organism
Bacillus licheniformis
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides (Ref. 4, PubMed:11109488). Shows high specificity for aromatic and hydrophobic amino acids in the P1 substrate position (PubMed:11109488). May play an important role in the degradation of feather keratin (PubMed:11109488).2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ca2+1 PublicationNote: Binds 2 calcium ions per subunit.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by p-chlorophenyl and 1-naphthyl boronic acid derivatives.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 1.6 sec(-1) with Suc-Ala2-Ala-pNA as substrate. kcat is 57 sec(-1) with Suc-Ala2-Phe-pNA as substrate. kcat is 97 sec(-1) with MeO-Suc-Ala2-Phe-pNA as substrate (Ref. 4). kcat is 0.990 sec(-1) with Suc-Gly2-Phe-pNA as substrate. kcat is 20.3 sec(-1) with Suc-Ala2-Phe-pNA as substrate. kcat is 646 sec(-1) with Suc-Ala2-Pro-Phe-pNA as substrate. kcat is 137 sec(-1) with Suc-Ala2-Pro-Leu-pNA as substrate. kcat is 5.31 sec(-1) with Suc-Ala2-Pro-Arg-pNA as substrate. kcat is 1.92 sec(-1) with Suc-Ala2-Pro-Glu-pNA as substrate. kcat is 375 sec(-1) with Suc-Ala-Glu-Pro-Phe-pNA as substrate (PubMed:11109488).2 Publications
  1. KM=1.2 mM for Suc-Ala2-Ala-pNA1 Publication
  2. KM=0.79 mM for Suc-Ala2-Phe-pNA1 Publication
  3. KM=0.851 mM for Suc-Ala2-Phe-pNA1 Publication
  4. KM=0.22 mM for MeO-Suc-Ala2-Phe-pNA1 Publication
  5. KM=5.6 mM for Suc-Gly2-Phe-pNA1 Publication
  6. KM=0.334 mM for Suc-Ala2-Pro-Phe-pNA1 Publication
  7. KM=0.062 mM for Suc-Ala2-Pro-Leu-pNA1 Publication
  8. KM=0.422 mM for Suc-Ala2-Pro-Arg-pNA1 Publication
  9. KM=0.245 mM for Suc-Ala2-Pro-Glu-pNA1 Publication
  10. KM=0.042 mM for Suc-Ala-Glu-Pro-Phe-pNA1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi107Calcium 11 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei137Charge relay systemPROSITE-ProRule annotation1
    Metal bindingi146Calcium 11 Publication1
    Active sitei168Charge relay systemPROSITE-ProRule annotation1
    Metal bindingi179Calcium 1; via carbonyl oxygen1 Publication1
    Metal bindingi181Calcium 11 Publication1
    Metal bindingi183Calcium 1; via carbonyl oxygen1 Publication1
    Metal bindingi185Calcium 1; via carbonyl oxygen1 Publication1
    Metal bindingi273Calcium 2; via carbonyl oxygen1 Publication1
    Metal bindingi275Calcium 2; via carbonyl oxygen1 Publication1
    Metal bindingi278Calcium 2; via carbonyl oxygen1 Publication1
    Active sitei325Charge relay systemPROSITE-ProRule annotation1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionHydrolase, Protease, Serine protease
    LigandCalcium, Metal-binding

    Enzyme and pathway databases

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P00780

    Protein family/group databases

    MEROPS protease database

    More...
    MEROPSi
    I09.001

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Subtilisin Carlsberg1 Publication (EC:3.4.21.622 Publications)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:subCImported
    Synonyms:apr
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBacillus licheniformis
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri1402 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    Keywords - Cellular componenti

    Secreted

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the ‘Pathology and Biotech’ section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

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

    Protein family/group databases

    Allergome; a platform for allergen knowledge

    More...
    Allergomei
    8254 Bac li Subtilisin

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL4299

    Drug and drug target database

    More...
    DrugBanki
    DB03316 1,4-Diethylene Dioxide
    DB03607 [(1R)-1-acetamido-2-(4-chlorophenyl)ethyl]-[(2S)-2-amino-3-hydroxy-3-oxo-propoxy]-dihydroxy-boron
    DB02560 [(1S)-1-acetamido-2-(4-chlorophenyl)ethyl]-[(2S)-2-amino-3-hydroxy-3-oxo-propoxy]-dihydroxy-boron
    DB02677 D-naphthyl-1-acetamido boronic acid alanine
    DB01942 Formic acid
    DB03290 L-naphthyl-1-acetamido boronic acid alanine

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 29Sequence analysisAdd BLAST29
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000002717930 – 1051 PublicationAdd BLAST76
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000027180106 – 379Subtilisin Carlsberg1 PublicationAdd BLAST274

    Keywords - PTMi

    Zymogen

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    Protein-protein interaction databases

    Protein interaction database and analysis system

    More...
    IntActi
    P00780, 2 interactors

    Molecular INTeraction database

    More...
    MINTi
    P00780

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P00780

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1379
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    SWISS-MODEL Interactive Workspace

    More...
    SWISS-MODEL-Workspacei
    Submit a new modelling project...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P00780

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini44 – 102Inhibitor I9Sequence analysisAdd BLAST59
    Domaini110 – 378Peptidase S8PROSITE-ProRule annotationAdd BLAST269

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the peptidase S8 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105RX7 Bacteria
    COG1404 LUCA

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd07477 Peptidases_S8_Subtilisin_subset, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.30.70.80, 1 hit
    3.40.50.200, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR000209 Peptidase_S8/S53_dom
    IPR036852 Peptidase_S8/S53_dom_sf
    IPR023827 Peptidase_S8_Asp-AS
    IPR022398 Peptidase_S8_His-AS
    IPR023828 Peptidase_S8_Ser-AS
    IPR015500 Peptidase_S8_subtilisin-rel
    IPR010259 S8pro/Inhibitor_I9
    IPR037045 S8pro/Inhibitor_I9_sf
    IPR034202 Subtilisin_Carlsberg-like

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF05922 Inhibitor_I9, 1 hit
    PF00082 Peptidase_S8, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00723 SUBTILISIN

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52743 SSF52743, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51892 SUBTILASE, 1 hit
    PS00136 SUBTILASE_ASP, 1 hit
    PS00137 SUBTILASE_HIS, 1 hit
    PS00138 SUBTILASE_SER, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P00780-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MMRKKSFWLG MLTAFMLVFT MAFSDSASAA QPAKNVEKDY IVGFKSGVKT
    60 70 80 90 100
    ASVKKDIIKE SGGKVDKQFR IINAAKAKLD KEALKEVKND PDVAYVEEDH
    110 120 130 140 150
    VAHALAQTVP YGIPLIKADK VQAQGFKGAN VKVAVLDTGI QASHPDLNVV
    160 170 180 190 200
    GGASFVAGEA YNTDGNGHGT HVAGTVAALD NTTGVLGVAP SVSLYAVKVL
    210 220 230 240 250
    NSSGSGSYSG IVSGIEWATT NGMDVINMSL GGASGSTAMK QAVDNAYAKG
    260 270 280 290 300
    VVVVAAAGNS GSSGNTNTIG YPAKYDSVIA VGAVDSNSNR ASFSSVGAEL
    310 320 330 340 350
    EVMAPGAGVY STYPTNTYAT LNGTSMASPH VAGAAALILS KHPNLSASQV
    360 370
    RNRLSSTATY LGSSFYYGKG LINVEAAAQ
    Length:379
    Mass (Da):38,867
    Last modified:September 18, 2019 - v2
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i38432C04FFA048C1
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti207S → T in CAB56500 (PubMed:3001653).Curated1
    Sequence conflicti233A → P in CAB56500 (PubMed:3001653).Curated1
    Sequence conflicti249K → R in CAB56500 (PubMed:3001653).Curated1
    Sequence conflicti249K → R AA sequence (PubMed:4967581).Curated1
    Sequence conflicti262 – 265SSGN → NSGS AA sequence (PubMed:4967581).Curated4
    Sequence conflicti316N → S in CAB56500 (PubMed:3001653).Curated1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    X03341 Genomic DNA Translation: CAB56500.1
    AF205189 Genomic DNA Translation: AAG31026.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A24111 SUBSCL

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X03341 Genomic DNA Translation: CAB56500.1
    AF205189 Genomic DNA Translation: AAG31026.1
    PIRiA24111 SUBSCL

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB 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[»]
    4C3UX-ray2.29A106-379[»]
    4C3VX-ray2.26A106-379[»]
    ModBaseiSearch...
    SWISS-MODEL-WorkspaceiSubmit a new modelling project...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    IntActiP00780, 2 interactors
    MINTiP00780

    Chemistry databases

    BindingDBiP00780
    ChEMBLiCHEMBL4299
    DrugBankiDB03316 1,4-Diethylene Dioxide
    DB03607 [(1R)-1-acetamido-2-(4-chlorophenyl)ethyl]-[(2S)-2-amino-3-hydroxy-3-oxo-propoxy]-dihydroxy-boron
    DB02560 [(1S)-1-acetamido-2-(4-chlorophenyl)ethyl]-[(2S)-2-amino-3-hydroxy-3-oxo-propoxy]-dihydroxy-boron
    DB02677 D-naphthyl-1-acetamido boronic acid alanine
    DB01942 Formic acid
    DB03290 L-naphthyl-1-acetamido boronic acid alanine

    Protein family/group databases

    Allergomei8254 Bac li Subtilisin
    MEROPSiI09.001

    Phylogenomic databases

    eggNOGiENOG4105RX7 Bacteria
    COG1404 LUCA

    Enzyme and pathway databases

    SABIO-RKiP00780

    Miscellaneous databases

    EvolutionaryTraceiP00780

    Family and domain databases

    CDDicd07477 Peptidases_S8_Subtilisin_subset, 1 hit
    Gene3Di3.30.70.80, 1 hit
    3.40.50.200, 1 hit
    InterProiView protein in InterPro
    IPR000209 Peptidase_S8/S53_dom
    IPR036852 Peptidase_S8/S53_dom_sf
    IPR023827 Peptidase_S8_Asp-AS
    IPR022398 Peptidase_S8_His-AS
    IPR023828 Peptidase_S8_Ser-AS
    IPR015500 Peptidase_S8_subtilisin-rel
    IPR010259 S8pro/Inhibitor_I9
    IPR037045 S8pro/Inhibitor_I9_sf
    IPR034202 Subtilisin_Carlsberg-like
    PfamiView protein in Pfam
    PF05922 Inhibitor_I9, 1 hit
    PF00082 Peptidase_S8, 1 hit
    PRINTSiPR00723 SUBTILISIN
    SUPFAMiSSF52743 SSF52743, 1 hit
    PROSITEiView protein in PROSITE
    PS51892 SUBTILASE, 1 hit
    PS00136 SUBTILASE_ASP, 1 hit
    PS00137 SUBTILASE_HIS, 1 hit
    PS00138 SUBTILASE_SER, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSUBC_BACLI
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P00780
    Secondary accession number(s): Q9F943
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: September 18, 2019
    Last modified: November 13, 2019
    This is version 151 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

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