Q9EY50 · FEMX_WEIVI

Function

function

Involved in the synthesis of the bacterial cell wall. Catalyzes the addition of alanine into the interchain peptide bridge of peptidoglycan precursor using aminoacyl-tRNA(Ala) as amino acid donor. This alanine is added to the epsilon-amino group of the L-lysine of the peptidoglycan UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine, in a ribosome-independent mechanism (PubMed:11083873, PubMed:12679335, PubMed:15901708, PubMed:23744707, PubMed:4248527).
Specific for UDP-N-acetyl-muramoyl-pentapeptide. Has no activity toward UDP-N-acetyl-muramoyl-tetrapeptide or UDP-N-acetyl-muramoyl-tripeptide (PubMed:15901708).
Also acts on L-seryl-tRNA(Ser) (PubMed:4248527).

Catalytic activity

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
15 μMtRNA(Ala)
1.7 μMtRNA(Ala)
42 μMUDP-N-acetyl-muramoyl-pentapeptide
79 μMUDP-N-acetyl-muramoyl-pentapeptide

pH Dependence

Optimum pH is 7.0-8.0.

Features

Showing features for binding site, site.

TypeIDPosition(s)Description
Binding site37-40substrate
Binding site104substrate
Site109Important for catalytic activity
Binding site212substrate
Binding site216substrate
Binding site257substrate
Site320Important for catalytic activity

GO annotations

AspectTerm
Molecular FunctionUDP-N-acetylmuramoylpentapeptide-lysine N6-alanyltransferase activity
Biological Processcell wall organization
Biological Processpeptidoglycan biosynthetic process
Biological Processregulation of cell shape

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    UDP-N-acetylmuramoylpentapeptide-lysine N(6)-alanyltransferase
  • EC number

Gene names

    • Name
      femX

Organism names

Accessions

  • Primary accession
    Q9EY50

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis29Loss of activity.
Mutagenesis29Loss of activity.
Mutagenesis37Loss of activity.
Mutagenesis37Reduces activity 150-fold.
Mutagenesis37Reduces activity 200-fold.
Mutagenesis39No effect on activity.
Mutagenesis40Reduces activity 2-fold.
Mutagenesis71Reduces activity 2-fold.
Mutagenesis73Reduces activity 2.5-fold.
Mutagenesis73Reduces activity 2.5-fold.
Mutagenesis104No effect on activity.
Mutagenesis109Reduces activity 200-fold.
Mutagenesis110Loss of activity.
Mutagenesis110Loss of activity.
Mutagenesis140Reduces activity 5-fold.
Mutagenesis144Reduces activity 9-fold.
Mutagenesis144Slightly reduces activity.
Mutagenesis196Reduces activity 4-fold.
Mutagenesis196Slightly reduces activity.
Mutagenesis205No effect on activity.
Mutagenesis207Reduces activity 11-fold.
Mutagenesis209Reduces activity 50-fold.
Mutagenesis210Reduces activity 2-fold.
Mutagenesis212Loss of activity.
Mutagenesis212Loss of activity.
Mutagenesis215No effect on activity.
Mutagenesis216Reduced activity.
Mutagenesis216Reduces activity 25-fold.
Mutagenesis216Loss of activity.
Mutagenesis257Reduces activity 2-fold.
Mutagenesis292Loss of activity.
Mutagenesis305Reduces activity 17-fold.
Mutagenesis305Reduces activity 33-fold.
Mutagenesis305Reduces activity 6-fold.
Mutagenesis305No effect on activity.
Mutagenesis306Loss of activity.
Mutagenesis306Reduces activity 12-fold.
Mutagenesis306Reduces activity 2.5-fold.
Mutagenesis306Reduces activity 200-fold.
Mutagenesis306Reduces activity 11-fold.
Mutagenesis306Loss of activity.
Mutagenesis316Reduces activity 3-fold.
Mutagenesis319Reduces activity 8-fold.
Mutagenesis319Reduces activity 20-fold.
Mutagenesis320Reduces activity 25-fold.

PTM/Processing

Features

Showing features for initiator methionine, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00004307792-336UDP-N-acetylmuramoylpentapeptide-lysine N6-alanyltransferase

Interaction

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the FemABX family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    336
  • Mass (Da)
    38,284
  • Last updated
    2001-03-01 v1
  • Checksum
    AFB94A2718148C3C
MPVLNLNDPQAVERYEEFMRQSPYGQVTQDLGWAKVKNNWEPVDVYLEDDQGAIIAAMSMLLGDTPTDKKFAYASKGPVMDVTDVDLLDRLVDEAVKALDGRAYVLRFDPEVAYSDEFNTTLQDHGYVTRNRNVADAGMHATIQPRLNMVLDLTKFPDAKTTLDLYPSKTKSKIKRPFRDGVEVHSGNSATELDEFFKTYTTMAERHGITHRPIEYFQRMQAAFDADTMRIFVAEREGKLLSTGIALKYGRKIWYMYAGSMDGNTYYAPYAVQSEMIQWALDTNTDLYDLGGIESESTDDSLYVFKHVFVKDAPREYIGEIDKVLDPEVYAELVKD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY008262
EMBL· GenBank· DDBJ
AAG21689.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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.
FeedbackHelp