Signal peptidase I

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

• Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins. EC:3.4.21.89

Sites

<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

• endopeptidase activity Source: EcoCyc <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Purification and characterization of leader (signal) peptidase from Escherichia coli."
    Zwizinski C., Wickner W.
    J Biol Chem 255:7973-7977(1980) [PubMed] [Europe PMC] [Abstract]
  • "Determination of Km and kcat for signal peptidase I using a full length secretory precursor, pro-OmpA-nuclease A."
    Chatterjee S., Suciu D., Dalbey R.E., Kahn P.C., Inouye M.
    J Mol Biol 245:311-314(1995) [PubMed] [Europe PMC] [Abstract]
• peptidase activity Source: EcoliWikiInferred from direct assayⁱ
  • "Identification of arginine residues important for the activity of Escherichia coli signal peptidase I."
    Kim Y.T., Kurita R., Kojima M., Nishii W., Tanokura M., Muramatsu T., Ito H., Takahashi K.
    Biol Chem 385:381-388(2004) [PubMed] [Europe PMC] [Abstract]
• serine-type endopeptidase activity Source: EcoCyc <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • Ref.7

    "Identification of potential active-site residues in the Escherichia coli leader peptidase."
    Sung M., Dalbey R.E.
    J. Biol. Chem. 267:13154-13159(1992) [PubMed] [Europe PMC] [Abstract]

    Cited for: MUTAGENESIS, ACTIVE SITES.
• toxic substance binding Source: EcoliWikiInferred from mutant phenotypeⁱ
  • "Cleavage of colicin D is necessary for cell killing and requires the inner membrane peptidase LepB."
    de Zamaroczy M., Mora L., Lecuyer A., Geli V., Buckingham R.H.
    Mol Cell 8:159-168(2001) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• protein processing Source: EcoliWikiInferred from mutant phenotypeⁱ
  • "Cleavage of colicin D is necessary for cell killing and requires the inner membrane peptidase LepB."
    de Zamaroczy M., Mora L., Lecuyer A., Geli V., Buckingham R.H.
    Mol Cell 8:159-168(2001) [PubMed] [Europe PMC] [Abstract]
  • "The identification of residues that control signal peptidase cleavage fidelity and substrate specificity."
    Karla A., Lively M.O., Paetzel M., Dalbey R.
    J Biol Chem 280:6731-6741(2005) [PubMed] [Europe PMC] [Abstract]
• proteolysis Source: EcoliWikiInferred from direct assayⁱ
  • "Kinetic and mechanistic studies of signal peptidase I from Escherichia coli."
    Stein R.L., Barbosa M.D., Bruckner R.
    Biochemistry 39:7973-7983(2000) [PubMed] [Europe PMC] [Abstract]
• signal peptide processing Source: EcoCycInferred from direct assayⁱ
  • "Purification and characterization of leader (signal) peptidase from Escherichia coli."
    Zwizinski C., Wickner W.
    J Biol Chem 255:7973-7977(1980) [PubMed] [Europe PMC] [Abstract]
  • "Determination of Km and kcat for signal peptidase I using a full length secretory precursor, pro-OmpA-nuclease A."
    Chatterjee S., Suciu D., Dalbey R.E., Kahn P.C., Inouye M.
    J Mol Biol 245:311-314(1995) [PubMed] [Europe PMC] [Abstract]

<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

Enzyme and pathway databases

Protein family/group databases

<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 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

• UniProt annotation
• GO - Cellular component

Topology

Keywords - Cellular componentⁱ

<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

Mutagenesis

Chemistry databases

<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

Amino acid modifications

Keywords - PTMⁱ

Proteomic databases

<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

Chemistry databases

<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

3D structure databases

Miscellaneous databases

<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

<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

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

        10         20         30         40         50
MANMFALILV IATLVTGILW CVDKFFFAPK RRERQAAAQA AAGDSLDKAT 
        60         70         80         90        100
LKKVAPKPGW LETGASVFPV LAIVLIVRSF IYEPFQIPSG SMMPTLLIGD 
       110        120        130        140        150
FILVEKFAYG IKDPIYQKTL IETGHPKRGD IVVFKYPEDP KLDYIKRAVG 
       160        170        180        190        200
LPGDKVTYDP VSKELTIQPG CSSGQACENA LPVTYSNVEP SDFVQTFSRR 
       210        220        230        240        250
NGGEATSGFF EVPKNETKEN GIRLSERKET LGDVTHRILT VPIAQDQVGM 
       260        270        280        290        300
YYQQPGQQLA TWIVPPGQYF MMGDNRDNSA DSRYWGFVPE ANLVGRATAI 
       310        320 
WMSFDKQEGE WPTGLRLSRI GGIH                             

Experimental Info

Sequence databases

Genome annotation databases

<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

• 100% Identity
• 90% Identity
• 50% Identity

<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

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<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 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

Documents

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