Q9EY50 · FEMX_WEIVI
- ProteinUDP-N-acetylmuramoylpentapeptide-lysine N(6)-alanyltransferase
- GenefemX
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids336 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
- L-alanyl-tRNA(Ala) + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine = H+ + tRNA(Ala) + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
15 μM | tRNA(Ala) | |||||
1.7 μM | tRNA(Ala) | |||||
42 μM | UDP-N-acetyl-muramoyl-pentapeptide | |||||
79 μM | UDP-N-acetyl-muramoyl-pentapeptide |
pH Dependence
Optimum pH is 7.0-8.0.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 37-40 | substrate | ||||
Sequence: KNNW | ||||||
Binding site | 104 | substrate | ||||
Sequence: Y | ||||||
Site | 109 | Important for catalytic activity | ||||
Sequence: D | ||||||
Binding site | 212 | substrate | ||||
Sequence: R | ||||||
Binding site | 216 | substrate | ||||
Sequence: Y | ||||||
Binding site | 257 | substrate | ||||
Sequence: Y | ||||||
Site | 320 | Important for catalytic activity | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | UDP-N-acetylmuramoylpentapeptide-lysine N6-alanyltransferase activity | |
Biological Process | cell wall organization | |
Biological Process | peptidoglycan biosynthetic process | |
Biological Process | regulation of cell shape |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameUDP-N-acetylmuramoylpentapeptide-lysine N(6)-alanyltransferase
- EC number
Gene names
Organism names
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Lactobacillaceae > Weissella
Accessions
- Primary accessionQ9EY50
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 29 | Loss of activity. | ||||
Sequence: Q → E | ||||||
Mutagenesis | 29 | Loss of activity. | ||||
Sequence: Q → T | ||||||
Mutagenesis | 37 | Loss of activity. | ||||
Sequence: K → M | ||||||
Mutagenesis | 37 | Reduces activity 150-fold. | ||||
Sequence: K → R | ||||||
Mutagenesis | 37 | Reduces activity 200-fold. | ||||
Sequence: K → R | ||||||
Mutagenesis | 39 | No effect on activity. | ||||
Sequence: N → L | ||||||
Mutagenesis | 40 | Reduces activity 2-fold. | ||||
Sequence: W → F | ||||||
Mutagenesis | 71 | Reduces activity 2-fold. | ||||
Sequence: F → L | ||||||
Mutagenesis | 73 | Reduces activity 2.5-fold. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 73 | Reduces activity 2.5-fold. | ||||
Sequence: Y → L | ||||||
Mutagenesis | 104 | No effect on activity. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 109 | Reduces activity 200-fold. | ||||
Sequence: D → N | ||||||
Mutagenesis | 110 | Loss of activity. | ||||
Sequence: P → F | ||||||
Mutagenesis | 110 | Loss of activity. | ||||
Sequence: P → H | ||||||
Mutagenesis | 140 | Reduces activity 5-fold. | ||||
Sequence: H → A | ||||||
Mutagenesis | 144 | Reduces activity 9-fold. | ||||
Sequence: Q → E | ||||||
Mutagenesis | 144 | Slightly reduces activity. | ||||
Sequence: Q → T | ||||||
Mutagenesis | 196 | Reduces activity 4-fold. | ||||
Sequence: F → L | ||||||
Mutagenesis | 196 | Slightly reduces activity. | ||||
Sequence: F → Y | ||||||
Mutagenesis | 205 | No effect on activity. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 207 | Reduces activity 11-fold. | ||||
Sequence: H → A | ||||||
Mutagenesis | 209 | Reduces activity 50-fold. | ||||
Sequence: I → A | ||||||
Mutagenesis | 210 | Reduces activity 2-fold. | ||||
Sequence: T → A | ||||||
Mutagenesis | 212 | Loss of activity. | ||||
Sequence: R → K | ||||||
Mutagenesis | 212 | Loss of activity. | ||||
Sequence: R → M | ||||||
Mutagenesis | 215 | No effect on activity. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 216 | Reduced activity. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 216 | Reduces activity 25-fold. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 216 | Loss of activity. | ||||
Sequence: Y → L | ||||||
Mutagenesis | 257 | Reduces activity 2-fold. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 292 | Loss of activity. | ||||
Sequence: G → V | ||||||
Mutagenesis | 305 | Reduces activity 17-fold. | ||||
Sequence: F → A | ||||||
Mutagenesis | 305 | Reduces activity 33-fold. | ||||
Sequence: F → L | ||||||
Mutagenesis | 305 | Reduces activity 6-fold. | ||||
Sequence: F → L | ||||||
Mutagenesis | 305 | No effect on activity. | ||||
Sequence: F → Y | ||||||
Mutagenesis | 306 | Loss of activity. | ||||
Sequence: K → A | ||||||
Mutagenesis | 306 | Reduces activity 12-fold. | ||||
Sequence: K → A | ||||||
Mutagenesis | 306 | Reduces activity 2.5-fold. | ||||
Sequence: K → C | ||||||
Mutagenesis | 306 | Reduces activity 200-fold. | ||||
Sequence: K → M | ||||||
Mutagenesis | 306 | Reduces activity 11-fold. | ||||
Sequence: K → N | ||||||
Mutagenesis | 306 | Loss of activity. | ||||
Sequence: K → R | ||||||
Mutagenesis | 316 | Reduces activity 3-fold. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 319 | Reduces activity 8-fold. | ||||
Sequence: G → S | ||||||
Mutagenesis | 319 | Reduces activity 20-fold. | ||||
Sequence: G → V | ||||||
Mutagenesis | 320 | Reduces activity 25-fold. | ||||
Sequence: E → Q |
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000430779 | 2-336 | UDP-N-acetylmuramoylpentapeptide-lysine N6-alanyltransferase | |||
Sequence: PVLNLNDPQAVERYEEFMRQSPYGQVTQDLGWAKVKNNWEPVDVYLEDDQGAIIAAMSMLLGDTPTDKKFAYASKGPVMDVTDVDLLDRLVDEAVKALDGRAYVLRFDPEVAYSDEFNTTLQDHGYVTRNRNVADAGMHATIQPRLNMVLDLTKFPDAKTTLDLYPSKTKSKIKRPFRDGVEVHSGNSATELDEFFKTYTTMAERHGITHRPIEYFQRMQAAFDADTMRIFVAEREGKLLSTGIALKYGRKIWYMYAGSMDGNTYYAPYAVQSEMIQWALDTNTDLYDLGGIESESTDDSLYVFKHVFVKDAPREYIGEIDKVLDPEVYAELVKD |
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length336
- Mass (Da)38,284
- Last updated2001-03-01 v1
- ChecksumAFB94A2718148C3C
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY008262 EMBL· GenBank· DDBJ | AAG21689.1 EMBL· GenBank· DDBJ | Genomic DNA |