Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

The annotation and conditions in this rule are derived from the following entries: P22188 (MURE_ECOLI), Q2FZP6 (MURE_STAA8), Q97PS1 (MURE_STRPN), Q9WY79 (MURE_THEMA), Q9A196 (MURE_STRP1)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_00208
    • taxon = Bacteria
    • fragment ≠ the sequence is fragmented

Special conditions

    • Subsequence at position 414 - 417 aligns to "D-N-P-R" in entry P22188
    • Subsequence at position 406 - 409 aligns to "D-[DN]-P-[NA]" in entry Q2FZP6
    • Subsequence at position 414 - 417 does not align to "D-N-P-R" in entry P22188
    • Subsequence at position 406 - 409 does not align to "D-[DN]-P-[NA]" in entry Q2FZP6
    • Subsequence at position 414 - 417 does not align to "D-N-P-R" in entry P22188
    • Subsequence at position 414 - 417 aligns to "D-N-P-R" in entry P22188
    • Subsequence at position 406 - 409 aligns to "D-[DN]-P-[NA]" in entry Q2FZP6
    • Subsequence at position 158 - 159 aligns to "[TS]-T" in entry P22188 (individually applies "UDP-MurNAc-L-Ala-D-Glu binding")
    • Subsequence at position 157 - 157 aligns to "[NQ]" in entry P22188 (individually applies "UDP-MurNAc-L-Ala-D-Glu")
    • Subsequence at position 27 - 27 aligns to "L" in entry P22188 (individually applies "UDP-MurNAc-L-Ala-D-Glu; via carbonyl oxygen")
    • Subsequence at position 29 - 29 aligns to "[ST]" in entry P22188 (individually applies "UDP-MurNAc-L-Ala-D-Glu")
    • Subsequence at position 193 - 193 aligns to "R" in entry P22188 (individually applies "UDP-MurNAc-L-Ala-D-Glu")
    • Subsequence at position 44 - 46 aligns to "H-[QRK]-[AVCT]" in entry P22188 (individually applies "UDP-MurNAc-L-Ala-D-Glu binding")
    • Subsequence at position 225 - 225 aligns to "K" in entry P22188 (individually applies "N6-carboxylysine")
    • Subsequence at position 185 - 185 aligns to "[ST]" in entry P22188 (individually applies "UDP-MurNAc-L-Ala-D-Glu")
    • Subsequence at position 191 - 191 aligns to "Q" in entry P22188 (individually applies "UDP-MurNAc-L-Ala-D-Glu")
    • Subsequence at position 116 - 122 aligns to "G-T-x-G-K-[ST]-[ST]" in entry P22188 (individually applies "ATP")
    • Subsequence at position 414 - 417 aligns to "D-N-P-R" in entry P22188
    • Subsequence at position 414 - 417 aligns to "D-N-x-R" in entry P22188 (individually applies "Meso-diaminopimelate binding")
    • Subsequence at position 469 - 469 aligns to "E" in entry P22188 (individually applies "Meso-diaminopimelate")
    • Subsequence at position 390 - 390 aligns to "R" in entry P22188 (individually applies "Meso-diaminopimelate")
    • Subsequence at position 465 - 465 aligns to "G" in entry P22188 (individually applies "Meso-diaminopimelate; via carbonyl oxygen")

... then these annotations are applied i

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:
    UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase (EC:6.3.2.13)
    Alternative name(s):
    Meso-A2pm-adding enzyme
    Meso-diaminopimelate-adding enzyme
    UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase
    UDP-MurNAc-tripeptide synthetase
    UDP-N-acetylmuramyl-tripeptide synthetase
  • Recommended name:
    UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase (EC:6.3.2.7)
    Alternative name(s):
    L-lysine-adding enzyme
    UDP-MurNAc-L-Ala-D-Glu:L-Lys ligase
    UDP-MurNAc-tripeptide synthetase
    UDP-N-acetylmuramyl-tripeptide synthetase
  • Recommended name:
    UDP-N-acetylmuramyl-tripeptide synthetase (EC:6.3.2.-)
    Alternative name(s):
    UDP-MurNAc-tripeptide synthetase

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

  • Name:murE

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

  • Carboxylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi

  • Pathwayi: peptidoglycan biosynthesis

    This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.
    View all proteins of this organism that are known to be involved in the pathway peptidoglycan biosynthesis and in Cell wall biogenesis.

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> describes the function(s) of a protein.<p><a href='/help/function' target='_top'>More...</a></p>Functioni

  • Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
  • Catalyzes the addition of L-lysine to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
  • Catalyzes the addition of an amino acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.

<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

<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

<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

<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi

  • Meso-diaminopimelate recognition motif (to residues corresponding to positions 414 - 417)
  • L-lysine recognition motif (to residues corresponding to positions 406 - 409)

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei

  • UDP-MurNAc-L-Ala-D-Glu (to residues corresponding to position 157)
  • UDP-MurNAc-L-Ala-D-Glu; via carbonyl oxygen (to residues corresponding to position 27)
  • UDP-MurNAc-L-Ala-D-Glu (to residues corresponding to position 29)
  • UDP-MurNAc-L-Ala-D-Glu (to residues corresponding to position 193)
  • UDP-MurNAc-L-Ala-D-Glu (to residues corresponding to position 185)
  • UDP-MurNAc-L-Ala-D-Glu (to residues corresponding to position 191)
  • Meso-diaminopimelate (to residues corresponding to position 469)
  • Meso-diaminopimelate (to residues corresponding to position 390)
  • Meso-diaminopimelate; via carbonyl oxygen (to residues corresponding to position 465)

<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni

  • UDP-MurNAc-L-Ala-D-Glu binding (to residues corresponding to positions 158 - 159)
  • UDP-MurNAc-L-Ala-D-Glu binding (to residues corresponding to positions 44 - 46)
  • Meso-diaminopimelate binding (to residues corresponding to positions 414 - 417)

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi

  • ATP (to residues corresponding to positions 116 - 122)

<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei

  • N6-carboxylysine (to residues corresponding to position 225)

<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

<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 (Gene Ontology) termsi

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again