Protein Domain : IPR013221

Type:  Domain Name:  Mur ligase, central
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) []. Short Name:  Mur_ligase_cen
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0 Child Features

1 Contains

DB identifier Type Name
IPR018109 Conserved_site Folylpolyglutamate synthetase, conserved site

3 Cross Referencess

Identifier
PF08245
G3DSA:3.40.1190.10
SSF53623

8 Found Ins

DB identifier Type Name
IPR005762 Family UDP-N-acetylmuramoylalanine-D-glutamate ligase
IPR005758 Family UDP-N-acetylmuramate--L-alanine ligase
IPR001645 Family Folylpolyglutamate synthetase
IPR005863 Family UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
IPR005761 Family UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase
IPR005757 Family Murein peptide ligase
IPR011810 Family Cyanophycin synthetase
IPR008337 Family Capsule biosynthesis protein CapB

2 GO Annotations

GO Term Gene Name
GO:0005524 IPR013221
GO:0009058 IPR013221

2 Ontology Annotations

GO Term Gene Name
GO:0005524 IPR013221
GO:0009058 IPR013221

0 Parent Features

3256 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
431032 D8TBA9 PAC:15419913 Selaginella moellendorffii 295  
148635 D8RNK3 PAC:15409337 Selaginella moellendorffii 532  
32076 D8RVZ6 PAC:15416911 Selaginella moellendorffii 440  
234236 D8SJ46 PAC:15401616 Selaginella moellendorffii 471  
119501 D8SKZ9 PAC:15412162 Selaginella moellendorffii 492  
229823 D8QPH8 PAC:15413718 Selaginella moellendorffii 492  
402370 D8QQE9 PAC:15403522 Selaginella moellendorffii 499  
402687 D8QMQ8 PAC:15405902 Selaginella moellendorffii 508  
133115 D8T6G4 PAC:15405904 Selaginella moellendorffii 515  
408505 D8R8I6 PAC:15422480 Selaginella moellendorffii 521  
75567 D8QMQ9 PAC:15413664 Selaginella moellendorffii 443  
90954 D8RC47 PAC:15416390 Selaginella moellendorffii 474  
evm.TU.contig_40876.1 PAC:16431544 Carica papaya 299  
evm.model.supercontig_120.13 PAC:16406948 Carica papaya 368  
evm.model.supercontig_138.10 PAC:16408443 Carica papaya 212  
evm.model.supercontig_138.6 PAC:16408494 Carica papaya 194  
evm.model.supercontig_3.50 PAC:16416813 Carica papaya 550  
evm.model.supercontig_346.3 PAC:16418089 Carica papaya 322  
evm.model.supercontig_74.56 PAC:16425748 Carica papaya 768  
evm.model.supercontig_776.1 PAC:16426172 Carica papaya 341  
evm.model.supercontig_8.34 PAC:16426626 Carica papaya 548  
evm.model.supercontig_85.118 PAC:16427428 Carica papaya 437  
30143.m001200 B9SE17 PAC:16819520 Ricinus communis 531  
30169.m006535 B9RIM1 PAC:16821335 Ricinus communis 552  
30190.m011226 B9RCC8 PAC:16823583 Ricinus communis 780  
32140.m000017 B9TIK7 PAC:16825307 Ricinus communis 101  
28470.m000437 B9SVS7 PAC:16800926 Ricinus communis 581  
29644.m000173 B9T4T4 PAC:16804543 Ricinus communis 1028  
28000.m000055 B9T905 PAC:16799755 Ricinus communis 850  
Cucsa.338340.2 PAC:16978740 Cucumis sativus 558  

6 Publications

First Author Title Year Journal Volume Pages PubMed ID
            9652408
            17139082
            17427948
            16595662
            16322581
            16934839