InterPro : IPR003447

Name  FemABX peptidyl transferase Short Name  FEMABX
Type  Family Description  The entry represents the FemABX peptidyl transferase family.FemABX peptidyl transferases catalyse the incorporation of amino acid(s) into the interchain peptide bridge of peptidoglycan using aminoacyl-tRNA as the amino acid donor, a reaction involved in the synthesis of the bacterial cell wall. The femABX enzymes catalyse the addition of amino acids to a peptidoglycan precursor, which in most cases is a lipid-linked sugar pentapeptide or, alternatively, a soluble nucleotide precursor for W. viridescens femX. The resulting branched peptide chain consists of one to five amino acids and is cross-linked to a pentapeptide of a neighbouring disaccharide chain by a transpeptidase in the final step of peptidoglycan synthesis. The interchain peptide and the femABX enzymes for their synthesis are found in several Gram-positive bacteria and in some Gram-negative, mainly pathogenic species. The femABX transferases differ by type, position and number of amino acids that are incoporated into the interchain. Some femABX proteins function as immunity factors that protect producers of interpeptide-specific endopeptidases against their own products. In addition, the interpeptide plays an important role in cell separation and virulence [, , , ].Some proteins known to belong to the femABX peptidyl transferase family:Staphylococcal femA and femB, factors essential for expression of methicillin resistance. FemA adds glycines 2 and 3 of the pentaglycine interpeptide, while femB adds glycines 4 and 5.Staphylococcal fmhB (for fem homolog) or femX, which incorporates the first glycine of the pentaglycine interchain peptidein peptidoglycan.Weissella viridescens femX, which catalyzes the transfer of an L-alanine from Ala-tRNA to the epsilon-amino group of L-lysine of UDP-MurNAc pentapeptide [, ].Streptococcus pneumoniae fibA/murM and fibB/murN, which synthesize branched structured cell wall muropeptides that are strain-specific.Staphylococcus capitis epr (endopeptidase resistance), which renders the cells resistant to glycylglycine endopeptidase by increasing the serine content and decreasing the glycine content of the interpeptide chains.
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

2 Contains

Id Name Short Name Type
IPR016181 Acyl-CoA N-acyltransferase Acyl_CoA_acyltransferase Domain
IPR010978 tRNA-binding arm tRNA-bd_arm Domain

0 Found In

0 Parent Features

4 Publications

First Author Title Year Journal Volume Pages
Biarrotte-Sorin S Crystal structures of Weissella viridescens FemX and its complex with UDP-MurNAc-pentapeptide: insights into FemABX family substrates recognition. 2004 Structure 12 257-67
Hegde SS FemABX family members are novel nonribosomal peptidyltransferases and important pathogen-specific drug targets. 2001 J Biol Chem 276 6998-7003
Rohrer S FemABX peptidyl transferases: a link between branched-chain cell wall peptide formation and beta-lactam resistance in gram-positive cocci. 2003 Antimicrob Agents Chemother 47 837-46
Hegde SS Kinetic and mechanistic characterization of recombinant Lactobacillus viridescens FemX (UDP-N-acetylmuramoyl pentapeptide-lysine N6-alanyltransferase). 2003 J Biol Chem 278 22861-7



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)