D-alanyl-D-alanine carboxypeptidase DacB

<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

Miscellaneous

<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

• 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

• carboxypeptidase 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
  • "Mutants of Escherichia coli lacking in highly penicillin-sensitive D-alanine carboxypeptidase activity."
    Matsuhashi M., Takagaki Y., Maruyama I.N., Tamaki S., Nishimura Y., Suzuki H., Ogino U., Hirota Y.
    Proc. Natl. Acad. Sci. U.S.A. 74:2976-2979(1977) [PubMed] [Europe PMC] [Abstract]
  • "On the process of cellular division in Escherichia coli: a series of mutants of E. coli altered in the penicillin-binding proteins."
    Suzuki H., Nishimura Y., Hirota Y.
    Proc. Natl. Acad. Sci. U.S.A. 75:664-668(1978) [PubMed] [Europe PMC] [Abstract]
• 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
  • Ref.6

    "Penicillin-binding protein 4 of Escherichia coli: molecular cloning of the dacB gene, controlled overexpression, and alterations in murein composition."
    Korat B., Mottl H., Keck W.
    Mol. Microbiol. 5:675-684(1991) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• penicillin binding Source: EcoCycInferred 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]
• serine-type D-Ala-D-Ala carboxypeptidase activity Source: EcoliWikiInferred from mutant phenotypeⁱ
  • "Mutants of Escherichia coli lacking in highly penicillin-sensitive D-alanine carboxypeptidase activity."
    Matsuhashi M., Takagaki Y., Maruyama I.N., Tamaki S., Nishimura Y., Suzuki H., Ogino U., Hirota Y.
    Proc. Natl. Acad. Sci. U.S.A. 74:2976-2979(1977) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• cell wall macromolecule catabolic process Source: EcoCycInferred from direct assayⁱ
  • Ref.6

    "Penicillin-binding protein 4 of Escherichia coli: molecular cloning of the dacB gene, controlled overexpression, and alterations in murein composition."
    Korat B., Mottl H., Keck W.
    Mol. Microbiol. 5:675-684(1991) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• cell wall organization Source: EcoCycInferred from direct assayⁱ
  • Ref.6

    "Penicillin-binding protein 4 of Escherichia coli: molecular cloning of the dacB gene, controlled overexpression, and alterations in murein composition."
    Korat B., Mottl H., Keck W.
    Mol. Microbiol. 5:675-684(1991) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• FtsZ-dependent cytokinesis Source: EcoCyc <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • "Effects of multiple deletions of murein hydrolases on viability, septum cleavage, and sensitivity to large toxic molecules in Escherichia coli."
    Heidrich C., Ursinus A., Berger J., Schwarz H., Holtje J.V.
    J. Bacteriol. 184:6093-6099(2002) [PubMed] [Europe PMC] [Abstract]
• peptidoglycan biosynthetic process Source: UniProtKB-UniPathway
• peptidoglycan catabolic process Source: EcoCycInferred from direct assayⁱ
  • Ref.6

    "Penicillin-binding protein 4 of Escherichia coli: molecular cloning of the dacB gene, controlled overexpression, and alterations in murein composition."
    Korat B., Mottl H., Keck W.
    Mol. Microbiol. 5:675-684(1991) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• peptidoglycan metabolic process Source: EcoCycInferred from direct assayⁱ
  • Ref.6

    "Penicillin-binding protein 4 of Escherichia coli: molecular cloning of the dacB gene, controlled overexpression, and alterations in murein composition."
    Korat B., Mottl H., Keck W.
    Mol. Microbiol. 5:675-684(1991) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• peptidoglycan turnover Source: EcoCycInferred from direct assayⁱ
  • Ref.6

    "Penicillin-binding protein 4 of Escherichia coli: molecular cloning of the dacB gene, controlled overexpression, and alterations in murein composition."
    Korat B., Mottl H., Keck W.
    Mol. Microbiol. 5:675-684(1991) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• regulation of cell shape Source: EcoCycInferred from genetic interactionⁱ
  • "Contributions of PBP 5 and DD-carboxypeptidase penicillin binding proteins to maintenance of cell shape in Escherichia coli."
    Nelson D.E., Young K.D.
    J. Bacteriol. 183:3055-3064(2001) [PubMed] [Europe PMC] [Abstract]
  • "FtsZ collaborates with penicillin binding proteins to generate bacterial cell shape in Escherichia coli."
    Varma A., Young K.D.
    J. Bacteriol. 186:6768-6774(2004) [PubMed] [Europe PMC] [Abstract]
  • "Endopeptidase penicillin-binding proteins 4 and 7 play auxiliary roles in determining uniform morphology of Escherichia coli."
    Meberg B.M., Paulson A.L., Priyadarshini R., Young K.D.
    J. Bacteriol. 186:8326-8336(2004) [PubMed] [Europe PMC] [Abstract]
• response to antibiotic Source: UniProtKB-KW

<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

Organism-specific databases

<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

• outer membrane-bounded periplasmic space Source: EcoliWikiInferred from mutant phenotypeⁱ
  • "Mutants of Escherichia coli lacking in highly penicillin-sensitive D-alanine carboxypeptidase activity."
    Matsuhashi M., Takagaki Y., Maruyama I.N., Tamaki S., Nishimura Y., Suzuki H., Ogino U., Hirota Y.
    Proc. Natl. Acad. Sci. U.S.A. 74:2976-2979(1977) [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

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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

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

Region

<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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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.

        10         20         30         40         50
MRFSRFIIGL TSCIAFSVQA ANVDEYITQL PAGANLALMV QKVGASAPAI 
        60         70         80         90        100
DYHSQQMALP ASTQKVITAL AALIQLGPDF RFTTTLETKG NVENGVLKGD 
       110        120        130        140        150
LVARFGADPT LKRQDIRNMV ATLKKSGVNQ IDGNVLIDTS IFASHDKAPG 
       160        170        180        190        200
WPWNDMTQCF SAPPAAAIVD RNCFSVSLYS APKPGDMAFI RVASYYPVTM 
       210        220        230        240        250
FSQVRTLPRG SAEAQYCELD VVPGDLNRFT LTGCLPQRSE PLPLAFAVQD 
       260        270        280        290        300
GASYAGAILK DELKQAGITW SGTLLRQTQV NEPGTVVASK QSAPLHDLLK 
       310        320        330        340        350
IMLKKSDNMI ADTVFRMIGH ARFNVPGTWR AGSDAVRQIL RQQAGVDIGN 
       360        370        380        390        400
TIIADGSGLS RHNLIAPATM MQVLQYIAQH DNELNFISML PLAGYDGSLQ 
       410        420        430        440        450
YRAGLHQAGV DGKVSAKTGS LQGVYNLAGF ITTASGQRMA FVQYLSGYAV 
       460        470 
EPADQRNRRI PLVRFESRLY KDIYQNN                          

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

Protocols and materials 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. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
2. SIMILARITY comments
   Index of protein domains and families
3. Peptidase families
   Classification of peptidase families and list of entries
4. Escherichia coli
   Escherichia coli (strain K12): entries and cross-references to EcoGene
5. PATHWAY comments
   Index of metabolic and biosynthesis pathways