C1EPS7 · MRAY_BACC3
- ProteinPhospho-N-acetylmuramoyl-pentapeptide-transferase
- GenemraY
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids324 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Catalytic activity
- di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP
Cofactor
Pathway
Cell wall biogenesis; peptidoglycan biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | metal ion binding | |
Molecular Function | phospho-N-acetylmuramoyl-pentapeptide-transferase activity | |
Molecular Function | UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity | |
Biological Process | cell division | |
Biological Process | cell wall organization | |
Biological Process | peptidoglycan biosynthetic process | |
Biological Process | regulation of cell shape |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhospho-N-acetylmuramoyl-pentapeptide-transferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus > Bacillus cereus group
Accessions
- Primary accessionC1EPS7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 5-25 | Helical | ||||
Sequence: GLLVTAGVAFLISVALSPLFI | ||||||
Transmembrane | 52-72 | Helical | ||||
Sequence: PTMGGIVIYVSMMVTSLIMAI | ||||||
Transmembrane | 77-97 | Helical | ||||
Sequence: LGAEVSLLLLVTFGYGLIGFL | ||||||
Transmembrane | 122-142 | Helical | ||||
Sequence: VIAIAFFLIGKGQAFHTYIMI | ||||||
Transmembrane | 149-169 | Helical | ||||
Sequence: FELGWAYFVLVLFMLIGGSNA | ||||||
Transmembrane | 176-196 | Helical | ||||
Sequence: LDGLLSGTAAIAFGAFSIIAV | ||||||
Transmembrane | 201-221 | Helical | ||||
Sequence: FGVAIFCMAVVGAVLGFLVFN | ||||||
Transmembrane | 227-247 | Helical | ||||
Sequence: VFMGDTGSLALGGAIAAVAIL | ||||||
Transmembrane | 253-273 | Helical | ||||
Sequence: LLVIIGGVFVMETLSVIIQVI | ||||||
Transmembrane | 302-322 | Helical | ||||
Sequence: VVVTFWSVGFLLAVLGIYIGV |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000117162 | 1-324 | Phospho-N-acetylmuramoyl-pentapeptide-transferase | |||
Sequence: MLEQGLLVTAGVAFLISVALSPLFIPFLRKLKFGQSIRDEGPKSHQKKSGTPTMGGIVIYVSMMVTSLIMAIKFNHLGAEVSLLLLVTFGYGLIGFLDDYIKVVKKRNLGLTSKQKLVGQLVIAIAFFLIGKGQAFHTYIMIPGTDVKFELGWAYFVLVLFMLIGGSNAVNLTDGLDGLLSGTAAIAFGAFSIIAVAQEQFGVAIFCMAVVGAVLGFLVFNANPAKVFMGDTGSLALGGAIAAVAILLKQELLLVIIGGVFVMETLSVIIQVISFKTTGKRVFKMSPLHHHYELCGWSEWRVVVTFWSVGFLLAVLGIYIGVWM |
Structure
Family & Domains
Sequence similarities
Belongs to the glycosyltransferase 4 family. MraY subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length324
- Mass (Da)34,906
- Last updated2009-05-26 v1
- ChecksumFC5E78105473854E
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001407 EMBL· GenBank· DDBJ | ACO28829.1 EMBL· GenBank· DDBJ | Genomic DNA |