D-alanyl-D-alanine carboxypeptidase DacA

<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

• a β-lactam

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  + H₂O

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  = a substituted β-amino acid

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  EC:3.5.2.6
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  Source: Rhea

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  a β-lactam

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  H₂O

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  =

  a substituted β-amino acid

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• Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine. EC:3.4.16.4

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

• beta-lactamase 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%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Site-directed mutagenesis of proposed active-site residues of penicillin-binding protein 5 from Escherichia coli."
    van der Linden M.P., de Haan L., Dideberg O., Keck W.
    Biochem. J. 303:357-362(1994) [PubMed] [Europe PMC] [Abstract]
• carboxypeptidase activity Source: EcoCycInferred from direct assayⁱ
  • "Synthetic peptidoglycan substrates for penicillin-binding protein 5 of Gram-negative bacteria."
    Hesek D., Suvorov M., Morio K., Lee M., Brown S., Vakulenko S.B., Mobashery S.
    J. Org. Chem. 69:778-784(2004) [PubMed] [Europe PMC] [Abstract]
  • "Purification and properties of penicillin-binding proteins 5 and 6 from Escherichia coli membranes."
    Amanuma H., Strominger J.L.
    J. Biol. Chem. 255:11173-11180(1980) [PubMed] [Europe PMC] [Abstract]
• endopeptidase activity Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• penicillin binding Source: EcoCycInferred from direct assayⁱ
  • "Purification and sequencing of the active site tryptic peptide from penicillin-binding protein 5 from the dacA mutant strain of Escherichia coli (TMRL 1222)."
    Nicholas R.A., Ishino F., Park W., Matsuhashi M., Strominger J.L.
    J. Biol. Chem. 260:6394-6397(1985) [PubMed] [Europe PMC] [Abstract]
  • "Purification and properties of penicillin-binding proteins 5 and 6 from Escherichia coli membranes."
    Amanuma H., Strominger J.L.
    J. Biol. Chem. 255:11173-11180(1980) [PubMed] [Europe PMC] [Abstract]
• serine-type D-Ala-D-Ala carboxypeptidase activity Source: EcoliWikiInferred from direct assayⁱ
  • "Cytoplasmic high-level expression of a soluble, enzymatically active form of the Escherichia coli penicillin-binding protein 5 and purification by dye chromatography."
    van der Linden M.P., Mottl H., Keck W.
    Eur. J. Biochem. 204:197-202(1992) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• cell wall organization Source: UniProtKB-KW
• peptidoglycan biosynthetic process Source: UniProtKB-UniPathway
• peptidoglycan metabolic process Source: EcoCycInferred from direct assayⁱ
  • "Synthetic peptidoglycan substrates for penicillin-binding protein 5 of Gram-negative bacteria."
    Hesek D., Suvorov M., Morio K., Lee M., Brown S., Vakulenko S.B., Mobashery S.
    J. Org. Chem. 69:778-784(2004) [PubMed] [Europe PMC] [Abstract]
  • "Septal and lateral wall localization of PBP5, the major D,D-carboxypeptidase of Escherichia coli, requires substrate recognition and membrane attachment."
    Potluri L., Karczmarek A., Verheul J., Piette A., Wilkin J.M., Werth N., Banzhaf M., Vollmer W., Young K.D., Nguyen-Disteche M., den Blaauwen T.
    Mol. Microbiol. 77:300-323(2010) [PubMed] [Europe PMC] [Abstract]
  • "Purification and properties of penicillin-binding proteins 5 and 6 from Escherichia coli membranes."
    Amanuma H., Strominger J.L.
    J. Biol. Chem. 255:11173-11180(1980) [PubMed] [Europe PMC] [Abstract]
• regulation of cell shape Source: EcoCycInferred from direct assayⁱ
  • "Septal and lateral wall localization of PBP5, the major D,D-carboxypeptidase of Escherichia coli, requires substrate recognition and membrane attachment."
    Potluri L., Karczmarek A., Verheul J., Piette A., Wilkin J.M., Werth N., Banzhaf M., Vollmer W., Young K.D., Nguyen-Disteche M., den Blaauwen T.
    Mol. Microbiol. 77:300-323(2010) [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

GO - Cellular componentⁱ

• integral component of periplasmic side of plasma membrane Source: EcoCycInferred from direct assayⁱ
  • "Elucidation of the structure of the membrane anchor of penicillin-binding protein 5 of Escherichia coli."
    O'Daniel P.I., Zajicek J., Zhang W., Shi Q., Fisher J.F., Mobashery S.
    J. Am. Chem. Soc. 132:4110-4118(2010) [PubMed] [Europe PMC] [Abstract]
• integral component of plasma membrane Source: EcoliWikiInferred from direct assayⁱ
  • "Properties of the penicillin-binding proteins of Escherichia coli K12,."
    Spratt B.G.
    Eur. J. Biochem. 72:341-352(1977) [PubMed] [Europe PMC] [Abstract]
• outer membrane-bounded periplasmic space Source: EcoCycInferred from direct assayⁱ
  • "Activity-Related Conformational Changes in d,d-Carboxypeptidases Revealed by In Vivo Periplasmic Forster Resonance Energy Transfer Assay in Escherichia coli."
    Meiresonne N.Y., van der Ploeg R., Hink M.A., den Blaauwen T.
    mBio 8:0-0(2017) [PubMed] [Europe PMC] [Abstract]
  • "The C terminus of penicillin-binding protein 5 is essential for localisation to the E. coli inner membrane."
    Pratt J.M., Jackson M.E., Holland I.B.
    EMBO J. 5:2399-2405(1986) [PubMed] [Europe PMC] [Abstract]
• plasma membrane Source: EcoCycInferred from direct assayⁱ
  • "Precursor forms of penicillin-binding proteins 5 and 6 of E. coli cytoplasmic membrane."
    Pratt J.M., Holland I.B., Spratt B.G.
    Nature 293:307-309(1981) [PubMed] [Europe PMC] [Abstract]

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

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

<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.

<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 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.

        10         20         30         40         50
MNTIFSARIM KRLALTTALC TAFISAAHAD DLNIKTMIPG VPQIDAESYI 
        60         70         80         90        100
LIDYNSGKVL AEQNADVRRD PASLTKMMTS YVIGQAMKAG KFKETDLVTI 
       110        120        130        140        150
GNDAWATGNP VFKGSSLMFL KPGMQVPVSQ LIRGINLQSG NDACVAMADF 
       160        170        180        190        200
AAGSQDAFVG LMNSYVNALG LKNTHFQTVH GLDADGQYSS ARDMALIGQA 
       210        220        230        240        250
LIRDVPNEYS IYKEKEFTFN GIRQLNRNGL LWDNSLNVDG IKTGHTDKAG 
       260        270        280        290        300
YNLVASATEG QMRLISAVMG GRTFKGREAE SKKLLTWGFR FFETVNPLKV 
       310        320        330        340        350
GKEFASEPVW FGDSDRASLG VDKDVYLTIP RGRMKDLKAS YVLNSSELHA 
       360        370        380        390        400
PLQKNQVVGT INFQLDGKTI EQRPLVVLQE IPEGNFFGKI IDYIKLMFHH 

WFG                                                    

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautionⁱ

Natural variant

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