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mraY phospho-N-acetylmuramoyl-pentapeptide undecaprenyl phosphate (C55P) transferase [ Bacillus subtilis subsp. subtilis str. 168 ]

Gene ID: 939856, updated on 12-Feb-2021
Gene symbol
mraY
Gene description
phospho-N-acetylmuramoyl-pentapeptide undecaprenyl phosphate (C55P) transferase
Locus tag
BSU_15190
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Bacillus subtilis subsp. subtilis str. 168 (strain: 168, sub-species: subtilis, type-material: type strain of Bacillus subtilis)
Lineage
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus
Old locus tag
BSU15190
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Sequence:
NC_000964.3 (1587926..1588900)

NC_000964.3Genomic Context describing neighboring genes Neighboring gene transpeptidase penicillin-binding protein Neighboring gene UDP-N-acetylmuramoylalanyl-D-glutamate-2, 6-diaminopimelate ligase Neighboring gene UDP-N-acetylmuramoylalanyl-D-glutamate ligase Neighboring gene factor for spore cortex peptidoglycan synthesis (stage V sporulation)

Genomic Sequence:
NC_000964.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Bacillus subtilis MraY in detergent-free system of nanodiscs wrapped by styrene-maleic acid copolymers. Liu Y, et al. PLoS One, 2018. PMID 30395652, Free PMC Article
  2. New Insight into the Catalytic Mechanism of Bacterial MraY from Enzyme Kinetics and Docking Studies. Liu Y, et al. J Biol Chem, 2016 Jul 15. PMID 27226570, Free PMC Article
  3. Active site mapping of MraY, a member of the polyprenyl-phosphate N-acetylhexosamine 1-phosphate transferase superfamily, catalyzing the first membrane step of peptidoglycan biosynthesis. Al-Dabbagh B, et al. Biochemistry, 2008 Aug 26. PMID 18672909
  4. Bacillus subtilis, the model Gram-positive bacterium: 20 years of annotation refinement. Borriss R, et al. Microb Biotechnol, 2018 Jan. PMID 29280348, Free PMC Article
  5. An updated metabolic view of the Bacillus subtilis 168 genome. Belda E, et al. Microbiology (Reading), 2013 Apr. PMID 23429746

See all (7) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. We used a detergent free system to purify MraY.The predominantly alpha-helical secondary structure of the protein in styrene-maleic acid copolymer(SMA)-wrapped nanodiscs was more stable against heat denaturation compared to the micellar protein.
    Title: Bacillus subtilis MraY in detergent-free system of nanodiscs wrapped by styrene-maleic acid copolymers.
  2. The concomitant binding of both UDP-MurNAc-pentapeptide-DNS and C35-P to the enzyme is required before the release of the two products, Lipid I and UMP. We built a model of MraY and performed docking studies with the substrate C35-P (short-chain homolog of undecaprenyl phosphate) to further deepen our understanding of how MraY accommodates this lipid substrate.
    Title: New Insight into the Catalytic Mechanism of Bacterial MraY from Enzyme Kinetics and Docking Studies.
  3. Data show that the important residues for mraY activity appeared to be distributed in all the cytoplasmic segments, and that the invariant D98 residue that should be involved in the deprotonation of the lipid substrate during the catalytic process.
    Title: Active site mapping of MraY, a member of the polyprenyl-phosphate N-acetylhexosamine 1-phosphate transferase superfamily, catalyzing the first membrane step of peptidoglycan biosynthesis.
Submit: New GeneRIF Correction

Homology

Preferred Names
phospho-N-acetylmuramoyl-pentapeptide undecaprenyl phosphate (C55P) transferase
NP_389402.2
  • Evidence 1a: Function from experimental evidences in the studied strain; PubMedId: 12682299, 15131133, 15849754, 16850406, 9592129, 24895118, 26620564, 27312048; Product type e: enzyme

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000964.3 Reference assembly

    Range
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_389402.2 phospho-N-acetylmuramoyl-pentapeptide undecaprenyl phosphate (C55P) transferase [Bacillus subtilis subsp. subtilis str. 168]

    See identical proteins and their annotated locations for NP_389402.2

    Status: PROVISIONAL

    UniProtKB/Swiss-Prot
    Q03521
    Conserved Domains (1) summary
    PRK00108
    Location:1 → 320
    mraY; phospho-N-acetylmuramoyl-pentapeptide-transferase; Provisional
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
Q03521.2

Gene LinkOut

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Other Literature Sources
Molecular Biology Databases