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Links from Protein

Items: 12

1.

Mur ligase family protein

This HMM hits multiple proteins of peptidoglycan (murein) biosynthesis, such as MurC, MurD, MurE, and MurF of Escherichia coli.

GO Terms:
Molecular Function:
ATP binding (GO:0005524)
Biological Process:
biosynthetic process (GO:0009058)
Molecular Function:
acid-amino acid ligase activity (GO:0016881)
Date:
2024-08-14
Family Accession:
NF019850.5
Method:
HMM
2.

glutamate ligase domain-containing protein

This entry contains a number of related ligase enzymes which have EC numbers 6.3.2.* which includes: MurC (Swiss:P17952), MurD (Swiss:P14900), MurE (Swiss:P22188), MurF (Swiss:P11880), Mpl (Swiss:P37773) and FolC (Swiss:P08192). MurC, MurD, MurE and MurF catalyse consecutive steps in the synthesis of peptidoglycan. Peptidoglycan consists of a sheet of two sugar derivatives, with one of these N-acetylmuramic acid attaching to a small pentapeptide. The pentapeptide is is made of L-alanine, D-glutamic acid, Meso-diaminopimelic acid and D-alanyl alanine. The peptide moiety is synthesised by successively adding these amino acids to UDP-N-acetylmuramic acid. MurC transfers the L-alanine, MurD transfers the D-glutamate, MurE transfers the diaminopimelic acid, and MurF transfers the D-alanyl alanine [1,3,4]. 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) [2]. [1]. 9218784. Crystal structure of UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli. Bertrand JA, Auger G, Fanchon E, Martin L, Blanot D, van Heijenoort J, Dideberg O;. EMBO J 1997;16:3416-3425. [2]. 9652408. Molecular characterization of cyanophycin synthetase, the enzyme catalyzing the biosynthesis of the cyanobacterial reserve material multi-L-arginyl-poly-L-aspartate (cyanophycin). Ziegler K, Diener A, Herpin C, Richter R, Deutzmann R, Lockau W;. Eur J Biochem. 1998;254:154-159. [3]. 25130693. The biology of Mur ligases as an antibacterial target. Ko. TRUNCATED at 1650 bytes (from Pfam)

GO Terms:
Biological Process:
biosynthetic process (GO:0009058)
Molecular Function:
acid-amino acid ligase activity (GO:0016881)
Date:
2024-10-16
Family Accession:
NF014874.5
Method:
HMM
3.

Mur ligase domain-containing protein

This family contains a number of related ligase enzymes which have EC numbers 6.3.2.*. This family includes: MurC (Swiss:P17952), MurD (Swiss:P14900), MurE (Swiss:P22188), MurF (Swiss:P11880), Mpl (Swiss:P37773) and FolC (Swiss:P08192). MurC, MurD, Mure and MurF catalyse consecutive steps in the synthesis of peptidoglycan. Peptidoglycan consists of a sheet of two sugar derivatives, with one of these N-acetylmuramic acid attaching to a small pentapeptide. The pentapeptide is is made of L-alanine, D-glutamic acid, Meso-diaminopimelic acid and D-alanyl alanine. The peptide moiety is synthesised by successively adding these amino acids to UDP-N-acetylmuramic acid. MurC transfers the L-alanine, MurD transfers the D-glutamate, MurE transfers the diaminopimelic acid, and MurF transfers the D-alanyl alanine. This family also includes Folylpolyglutamate synthase that transfers glutamate to folylpolyglutamate. [1]. 9218784. Crystal structure of UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli. Bertrand JA, Auger G, Fanchon E, Martin L, Blanot D, van Heijenoort J, Dideberg O;. EMBO J 1997;16:3416-3425. (from Pfam)

GO Terms:
Biological Process:
biosynthetic process (GO:0009058)
Molecular Function:
acid-amino acid ligase activity (GO:0016881)
Date:
2024-10-16
Family Accession:
NF013396.5
Method:
HMM
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.
new record, indexing in progress
Family Accession:
10.

UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase

UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein

Date:
2023-03-08
Family Accession:
11484936
Method:
Sparcle
11.

UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase

This family consists of the strictly bacterial MurF gene of peptidoglycan biosynthesis. This enzyme is almost always UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanyl ligase, but in a few species, MurE adds lysine rather than diaminopimelate. This enzyme acts on the product from MurE activity, and so is also subfamily rather than equivalog. Staphylococcus aureus is an example of species in this MurF protein would differ.

Gene:
murF
GO Terms:
Molecular Function:
ATP binding (GO:0005524)
Molecular Function:
UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-alanine ligase activity (GO:0008766)
Biological Process:
peptidoglycan biosynthetic process (GO:0009252)
Molecular Function:
UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity (GO:0047480)
Biological Process:
cell wall organization (GO:0071555)
Date:
2024-05-30
Family Accession:
TIGR01143.1
Method:
HMM
12.

UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase

Gene:
murF
GO Terms:
Molecular Function:
ATP binding (GO:0005524)
Biological Process:
biosynthetic process (GO:0009058)
Molecular Function:
UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity (GO:0047480)
Biological Process:
cell wall organization (GO:0071555)
Date:
2021-08-30
Family Accession:
NF008041.0
Method:
HMM
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