Peptidoglycan D,D-transpeptidase MrdA

<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

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

  <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesⁱ

  • HAMAP-Rule:MF_02081

  1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.10

    "Peptidoglycan synthetic activities in membranes of Escherichia coli caused by overproduction of penicillin-binding protein 2 and rodA protein."
    Ishino F., Park W., Tomioka S., Tamaki S., Takase I., Kunugita K., Matsuzawa H., Asoh S., Ohta T., Spratt B.G.
    J. Biol. Chem. 261:7024-7031(1986) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY, SUBCELLULAR LOCATION.

  EC:3.4.16.4

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

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

• drug binding 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
  • "In vitro and in vivo activities of AM-112, a novel oxapenem."
    Jamieson C.E., Lambert P.A., Simpson I.N.
    Antimicrob. Agents Chemother. 47:1652-1657(2003) [PubMed] [Europe PMC] [Abstract]
  • "Target affinities of faropenem to and its impact on the morphology of gram-positive and gram-negative bacteria."
    Dalhoff A., Nasu T., Okamoto K.
    Chemotherapy 49:172-183(2003) [PubMed] [Europe PMC] [Abstract]
  • "Binding of ceftobiprole and comparators to the penicillin-binding proteins of Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Streptococcus pneumoniae."
    Davies T.A., Page M.G., Shang W., Andrew T., Kania M., Bush K.
    Antimicrob. Agents Chemother. 51:2621-2624(2007) [PubMed] [Europe PMC] [Abstract]
  • "Affinity of doripenem and comparators to penicillin-binding proteins in Escherichia coli and Pseudomonas aeruginosa."
    Davies T.A., Shang W., Bush K., Flamm R.K.
    Antimicrob. Agents Chemother. 52:1510-1512(2008) [PubMed] [Europe PMC] [Abstract]
• penicillin binding Source: EcoliWiki <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%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • Ref.8

    "Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12."
    Spratt B.G.
    Proc. Natl. Acad. Sci. U.S.A. 72:2999-3003(1975) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, ACTIVITY REGULATION.
• peptidoglycan L,D-transpeptidase activity Source: EcoliWikiInferred from direct assayⁱ
  • "A mecillinam-sensitive peptidoglycan crosslinking reaction in Escherichia coli."
    Ishino F., Tamaki S., Spratt B.G., Matsuhashi M.
    Biochem. Biophys. Res. Commun. 109:689-696(1982) [PubMed] [Europe PMC] [Abstract]
• serine-type D-Ala-D-Ala carboxypeptidase activity Source: EcoCycInferred from direct assayⁱ
  • Ref.10

    "Peptidoglycan synthetic activities in membranes of Escherichia coli caused by overproduction of penicillin-binding protein 2 and rodA protein."
    Ishino F., Park W., Tomioka S., Tamaki S., Takase I., Kunugita K., Matsuzawa H., Asoh S., Ohta T., Spratt B.G.
    J. Biol. Chem. 261:7024-7031(1986) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY, SUBCELLULAR LOCATION.

GO - Biological processⁱ

• cell wall organization Source: EcoCycInferred from mutant phenotypeⁱ
  • "Constitutive septal murein synthesis in Escherichia coli with impaired activity of the morphogenetic proteins RodA and penicillin-binding protein 2."
    de Pedro M.A., Donachie W.D., Holtje J.V., Schwarz H.
    J. Bacteriol. 183:4115-4126(2001) [PubMed] [Europe PMC] [Abstract]
  • "Growth of Escherichia coli: significance of peptidoglycan degradation during elongation and septation."
    Uehara T., Park J.T.
    J. Bacteriol. 190:3914-3922(2008) [PubMed] [Europe PMC] [Abstract]
  • "Effects of temperature inactivation of penicillin-binding protein 2 on envelope growth in Escherichia coli."
    Buchnik D., Woldringh C.L., Zaritsky A.
    Ann. Inst. Pasteur Microbiol. 138:537-547(1987) [PubMed] [Europe PMC] [Abstract]
• peptidoglycan biosynthetic process Source: EcoCycInferred from mutant phenotypeⁱ
  • "Growth of Escherichia coli: significance of peptidoglycan degradation during elongation and septation."
    Uehara T., Park J.T.
    J. Bacteriol. 190:3914-3922(2008) [PubMed] [Europe PMC] [Abstract]
  • "Modified peptidoglycan chemical composition in shape-altered Escherichia coli."
    Signoretto C., Di Stefano F., Canepari P.
    Microbiology (Reading, Engl.) 142:1919-1926(1996) [PubMed] [Europe PMC] [Abstract]
• regulation of cell shape Source: EcoliWikiInferred from mutant phenotypeⁱ
  • Ref.8

    "Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12."
    Spratt B.G.
    Proc. Natl. Acad. Sci. U.S.A. 72:2999-3003(1975) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, ACTIVITY REGULATION.
• response to antibiotic Source: EcoliWikiInferred from mutant phenotypeⁱ
  • Ref.8

    "Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12."
    Spratt B.G.
    Proc. Natl. Acad. Sci. U.S.A. 72:2999-3003(1975) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, ACTIVITY REGULATION.
• response to drug Source: EcoCycInferred from direct assayⁱ
  • "Binding of ceftobiprole and comparators to the penicillin-binding proteins of Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Streptococcus pneumoniae."
    Davies T.A., Page M.G., Shang W., Andrew T., Kania M., Bush K.
    Antimicrob. Agents Chemother. 51:2621-2624(2007) [PubMed] [Europe PMC] [Abstract]
  • "Affinity of doripenem and comparators to penicillin-binding proteins in Escherichia coli and Pseudomonas aeruginosa."
    Davies T.A., Shang W., Bush K., Flamm R.K.
    Antimicrob. Agents Chemother. 52:1510-1512(2008) [PubMed] [Europe PMC] [Abstract]
  • "Growth of Escherichia coli: significance of peptidoglycan degradation during elongation and septation."
    Uehara T., Park J.T.
    J. Bacteriol. 190:3914-3922(2008) [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

<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

Topology

GO - Cellular componentⁱ

• integral component of plasma membrane Source: EcoliWikiInferred from direct assayⁱ
  • Ref.8

    "Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12."
    Spratt B.G.
    Proc. Natl. Acad. Sci. U.S.A. 72:2999-3003(1975) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, ACTIVITY REGULATION.

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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypeⁱ

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

<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
MKLQNSFRDY TAESALFVRR ALVAFLGILL LTGVLIANLY NLQIVRFTDY 
        60         70         80         90        100
QTRSNENRIK LVPIAPSRGI IYDRNGIPLA LNRTIYQIEM MPEKVDNVQQ 
       110        120        130        140        150
TLDALRSVVD LTDDDIAAFR KERARSHRFT SIPVKTNLTE VQVARFAVNQ 
       160        170        180        190        200
YRFPGVEVKG YKRRYYPYGS ALTHVIGYVS KINDKDVERL NNDGKLANYA 
       210        220        230        240        250
ATHDIGKLGI ERYYEDVLHG QTGYEEVEVN NRGRVIRQLK EVPPQAGHDI 
       260        270        280        290        300
YLTLDLKLQQ YIETLLAGSR AAVVVTDPRT GGVLALVSTP SYDPNLFVDG 
       310        320        330        340        350
ISSKDYSALL NDPNTPLVNR ATQGVYPPAS TVKPYVAVSA LSAGVITRNT 
       360        370        380        390        400
TLFDPGWWQL PGSEKRYRDW KKWGHGRLNV TRSLEESADT FFYQVAYDMG 
       410        420        430        440        450
IDRLSEWMGK FGYGHYTGID LAEERSGNMP TREWKQKRFK KPWYQGDTIP 
       460        470        480        490        500
VGIGQGYWTA TPIQMSKALM ILINDGIVKV PHLLMSTAED GKQVPWVQPH 
       510        520        530        540        550
EPPVGDIHSG YWELAKDGMY GVANRPNGTA HKYFASAPYK IAAKSGTAQV 
       560        570        580        590        600
FGLKANETYN AHKIAERLRD HKLMTAFAPY NNPQVAVAMI LENGGAGPAV 
       610        620        630 
GTLMRQILDH IMLGDNNTDL PAENPAVAAA EDH                   

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

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