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Protein Domain : IPR013221

Name  Mur ligase, central Short Name  Mur_ligase_cen
Type  Domain Description  The bacterial cell wall provides strength and rigidity to counteract internal osmotic pressure, and protection against the environment. The peptidoglycan layer gives the cell wall its strength, and helps maintain the overall shape of the cell. The basic peptidoglycan structure of both Gram-positive and Gram-negative bacteria is comprised of a sheet of glycan chains connected by short cross-linking polypeptides. Biosynthesis of peptidoglycan is a multi-step (11-12 steps) process comprising three main stages:(1) formation of UDP-N-acetylmuramic acid (UDPMurNAc) from N-acetylglucosamine (GlcNAc).(2) addition of a short polypeptide chain to the UDPMurNAc.(3) addition of a second GlcNAc to the disaccharide-pentapeptide building block and transport of this unit through the cytoplasmic membrane and incorporation into the growing peptidoglycan layer.Stage two involves four key Mur ligase enzymes: MurC () [], MurD () [], MurE () []and MurF () []. These four Mur ligases are responsible for the successive additions of L-alanine, D-glutamate, meso-diaminopimelate or L-lysine, and D-alanyl-D-alanine to UDP-N-acetylmuramic acid. All four Mur ligases are topologically similar to one another, even though they display low sequence identity. They are each composed of three domains: an N-terminal Rossmann-fold domain responsible for binding the UDPMurNAc substrate; a central domain (similar to ATP-binding domains of several ATPases and GTPases); and a C-terminal domain (similar to dihydrofolate reductase fold) that appears to be associated with binding the incoming amino acid. The conserved sequence motifs found in the four Mur enzymes also map to other members of the Mur ligase family, including folylpolyglutamate synthetase, cyanophycin synthetase and the capB enzyme from Bacillales []. This entry represents the C-terminal domain from all four stage 2 Mur enzymes: UDP-N-acetylmuramate-L-alanine ligase (MurC), UDP-N-acetylmuramoylalanine-D-glutamate ligase (MurD), UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase (MurE), and UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase (MurF). This entry also includes folylpolyglutamate synthase that transfers glutamate to folylpolyglutamate and cyanophycin synthetase that catalyses the biosynthesis of the cyanobacterial reserve material multi-L-arginyl-poly-L-aspartate (cyanophycin) [].
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Publication Counts Displayer

0 Child Features

1 Contains

DB identifier Name Short Name Type
IPR018109 Folylpolyglutamate synthetase, conserved site Folylpolyglutamate_synth_CS Conserved_site

3 Cross References

Identifier
Source . Name
Subject . Primary Identifier
PF08245 PFAM IPR013221
G3DSA:3.40.1190.10 GENE3D IPR013221
SSF53623 SSF IPR013221

3 Data Sets

Name URL
TrEMBL data set http://www.ebi.ac.uk/trembl/
InterPro data set  
InterPro GO Annotation data set  

8 Found In

DB identifier Name Short Name Type
IPR001645 Folylpolyglutamate synthetase Folylpolyglutamate_synth Family
IPR011810 Cyanophycin synthetase Cya_phycin_syn Family
IPR005863 UDP-MurNAc-pentapeptide synthetase UDP-N-AcMur-pentapeptide_synth Family
IPR005761 UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase UDP-N-AcMur-Glu-dNH2Pim_ligase Family
IPR005762 UDP-N-acetylmuramoylalanine-D-glutamate ligase UDP-N-AcMur-Glu_ligase Family
IPR005758 UDP-N-acetylmuramate-alanine ligase UDP-N-AcMur_Ala_ligase Family
IPR005757 Murein peptide ligase Murein_peptide_ligase Family
IPR008337 Capsule biosynthesis protein CapB Capsule_biosynth_CapB Family

2 GO Annotation


Subject . Secondary Identifier
Subject . Name
Subject . Symbol
Ontology Term . Identifier
Ontology Term . Name
Mur ligase, central   GO:0005524 ATP binding
Mur ligase, central   GO:0009058 biosynthetic process

2 Ontology Annotations


Subject . Secondary Identifier
Subject . Name
Subject . Symbol
Ontology Term . Identifier
Ontology Term . Name
Mur ligase, central   GO:0005524 ATP binding
Mur ligase, central   GO:0009058 biosynthetic process

0 Parent Features

20 Proteins

DB identifier Primary Accession
Organism . Name
FBpp0073488 Q9VYL1 Drosophila melanogaster
FBpp0077198 Q9VQW0 Drosophila melanogaster
FBpp0276118 B5DNJ3 Drosophila pseudoobscura
FBpp0273355 Q29J67 Drosophila pseudoobscura
FBpp0273505 B5DLC2 Drosophila pseudoobscura
FBpp0274441 B5DNJ4 Drosophila pseudoobscura
FBpp0164473 B4KHD4 Drosophila mojavensis
FBpp0165602 B4L6K6 Drosophila mojavensis
FBpp0231177 B4M880 Drosophila virilis
FBpp0231681 B4LU85 Drosophila virilis
FBpp0259793 B4NYG6 Drosophila yakuba
FBpp0262028 B4Q1P0 Drosophila yakuba
A8X7Y9_CAEBR A8X7Y9 Caenorhabditis briggsae
H2WNP9_CAEJA H2WNP9 Caenorhabditis japonica
G0MLK2_CAEBE G0MLK2 Caenorhabditis brenneri
FOLC_CAEEL Q09509 Caenorhabditis elegans
FOLC_CAEEL-3 Q09509-3 Caenorhabditis elegans
FOLC_CAEEL-2 Q09509-2 Caenorhabditis elegans
Q8MRU3_DROME Q8MRU3 Drosophila melanogaster
E3LYQ3_CAERE E3LYQ3 Caenorhabditis remanei




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