Identification
Name:Phospho-N-acetylmuramoyl-pentapeptide-transferase
Synonyms:
  • UDP-MurNAc-pentapeptide phosphotransferase
Gene Name:mraY
Enzyme Class:
Biological Properties
General Function:Involved in phospho-N-acetylmuramoyl-pentapeptide-transferase activity
Specific Function:First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan
Cellular Location:Cell inner membrane; Multi-pass membrane protein
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
SMPDB Reactions:
1.0Thumb+1.0di-trans,octa-cis-undecaprenyl phosphate1.0Thumb+1.0Undecaprenyl-diphospho-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine+1.0Thumb
1.0UDP-N-acetyl-α-D-muramoyl-L-alanyl-γ-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + 1.0di-trans,octa-cis-undecaprenyl phosphate → 1.0Uridine 5'-monophosphate + 1.0Undecaprenyl-diphospho-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + 1.0Undecaprenyl-diphospho-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine
ReactionCard
1.0Thumb+1.0di-trans,octa-cis-undecaprenyl phosphate1.0Thumb+1.0Thumb
EcoCyc Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
Complex Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB20310Di-trans,poly-cis-undecaprenyl phosphateMetaboCard
ECMDB23030Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenolMetaboCard
ECMDB20173MurAc(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala)-diphospho-undecaprenolMetaboCard
ECMDB20290N-Acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamineMetaboCard
ECMDB20257N-Acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenolMetaboCard
ECMDB23138UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)MetaboCard
ECMDB24251UDP-N-acetyl-α-D-muramoyl-L-alanyl-γ-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanineMetaboCard
ECMDB20204UDP-N-Acetylmuramoyl-L-alanyl-D-glutamyl-6-carboxy-L-lysyl-D-alanyl-D-alanineMetaboCard
ECMDB20205UDP-N-Acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanineMetaboCard
ECMDB20208Undecaprenyl phosphateMetaboCard
ECMDB20210Undecaprenyl-diphospho-N-acetylmuramoyl-(N-acetylglucosamine)-L-alanyl-D-glutaminyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanineMetaboCard
ECMDB20216Undecaprenyl-diphospho-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanineMetaboCard
ECMDB00288Uridine 5'-monophosphateMetaboCard
GO Classification:
Component
cell part
integral to membrane
intrinsic to membrane
membrane
membrane part
Function
catalytic activity
phospho-N-acetylmuramoyl-pentapeptide-transferase activity
phosphotransferase activity, for other substituted phosphate groups
transferase activity
transferase activity, transferring phosphorus-containing groups
Process
aminoglycan metabolic process
carbohydrate metabolic process
glycosaminoglycan metabolic process
metabolic process
peptidoglycan biosynthetic process
peptidoglycan metabolic process
polysaccharide metabolic process
primary metabolic process
Gene Properties
Blattner:b0087
Gene OrientationClockwise
Centisome Percentage:2.07
Left Sequence End96002
Right Sequence End97084
Gene Sequence:
>1083 bp
ATGTTAGTTTGGCTGGCCGAACATTTGGTCAAATATTATTCCGGCTTTAACGTCTTTTCC
TATCTGACGTTTCGCGCCATCGTCAGCCTGCTGACCGCGCTGTTCATCTCATTGTGGATG
GGCCCGCGTATGATTGCTCATTTGCAAAAACTTTCCTTTGGTCAGGTGGTGCGTAACGAC
GGTCCTGAATCACACTTCAGCAAGCGCGGTACGCCGACCATGGGCGGGATTATGATCCTG
ACGGCGATTGTGATCTCCGTACTGCTGTGGGCTTACCCGTCCAATCCGTACGTCTGGTGC
GTGTTGGTGGTGCTGGTAGGTTACGGTGTTATTGGCTTTGTTGATGATTATCGCAAAGTG
GTGCGTAAAGACACCAAAGGGTTGATCGCTCGTTGGAAGTATTTCTGGATGTCGGTCATT
GCGCTGGGTGTCGCCTTCGCCCTGTACCTTGCCGGCAAAGACACGCCCGCAACGCAGCTG
GTGGTCCCATTCTTTAAAGATGTGATGCCGCAGCTGGGGCTGTTCTACATTCTGCTGGCT
TACTTCGTCATTGTGGGTACTGGCAACGCGGTAAACCTGACCGATGGTCTCGACGGCCTG
GCAATTATGCCGACCGTATTTGTCGCCGGTGGTTTTGCGCTGGTGGCGTGGGCGACCGGC
AATATGAACTTTGCCAGCTACTTGCATATACCGTATCTGCGACACGCCGGGGAACTGGTT
ATTGTCTGTACCGCGATAGTCGGGGCAGGACTGGGCTTCCTGTGGTTTAACACCTATCCG
GCGCAGGTCTTTATGGGCGATGTAGGTTCGCTGGCGTTAGGTGGTGCGTTAGGCATTATC
GCCGTACTGCTACGTCAGGAATTCCTGCTGGTGATTATGGGGGGCGTGTTCGTGGTAGAA
ACGCTTTCTGTCATCCTGCAGGTCGGCTCCTTTAAACTGCGCGGACAACGTATTTTCCGC
ATGGCACCGATTCATCACCACTATGAACTGAAAGGCTGGCCGGAACCGCGCGTCATTGTG
CGTTTCTGGATTATTTCGCTGATGCTGGTTCTGATTGGTCTGGCAACGCTGAAGGTACGT
TAA
Protein Properties
Pfam Domain Function:
Protein Residues:360
Protein Molecular Weight:39875
Protein Theoretical pI:10
Signaling Regions:
  • None
Transmembrane Regions:
  • 19-45
  • 77-90
  • 97-113
  • 134-156
  • 174-188
  • 200-220
  • 239-251
  • 271-284
  • 288-299
  • 342-357
Protein Sequence:
>Phospho-N-acetylmuramoyl-pentapeptide-transferase
MLVWLAEHLVKYYSGFNVFSYLTFRAIVSLLTALFISLWMGPRMIAHLQKLSFGQVVRND
GPESHFSKRGTPTMGGIMILTAIVISVLLWAYPSNPYVWCVLVVLVGYGVIGFVDDYRKV
VRKDTKGLIARWKYFWMSVIALGVAFALYLAGKDTPATQLVVPFFKDVMPQLGLFYILLA
YFVIVGTGNAVNLTDGLDGLAIMPTVFVAGGFALVAWATGNMNFASYLHIPYLRHAGELV
IVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGALGIIAVLLRQEFLLVIMGGVFVVE
TLSVILQVGSFKLRGQRIFRMAPIHHHYELKGWPEPRVIVRFWIISLMLVLIGLATLKVR
References
External Links:
ResourceLink
Uniprot ID:P0A6W3
Uniprot Name:MRAY_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321968
Ecogene ID:EG10604
Ecocyc:EG10604
ColiBase:b0087
Kegg Gene:b0087
EchoBASE ID:EB0599
CCDB:MRAY_ECOLI
BacMap:16128080
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Bouhss, A., Mengin-Lecreulx, D., Le Beller, D., Van Heijenoort, J. (1999). "Topological analysis of the MraY protein catalysing the first membrane step of peptidoglycan synthesis." Mol Microbiol 34:576-585. Pubmed: 10564498
  • Daley, D. O., Rapp, M., Granseth, E., Melen, K., Drew, D., von Heijne, G. (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308:1321-1323. Pubmed: 15919996
  • Geis, A., Plapp, R. (1978). "Phospho-N-acetylmuramoyl-pentapeptide-transferase of Escherichia coli K12. Properties of the membrane-bound and the extracted and partially purified enzyme." Biochim Biophys Acta 527:414-424. Pubmed: 215212
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Ikeda, M., Wachi, M., Ishino, F., Matsuhashi, M. (1990). "Nucleotide sequence involving murD and an open reading frame ORF-Y spacing murF and ftsW in Escherichia coli." Nucleic Acids Res 18:1058. Pubmed: 2179861
  • Ikeda, M., Wachi, M., Jung, H. K., Ishino, F., Matsuhashi, M. (1991). "The Escherichia coli mraY gene encoding UDP-N-acetylmuramoyl-pentapeptide: undecaprenyl-phosphate phospho-N-acetylmuramoyl-pentapeptide transferase." J Bacteriol 173:1021-1026. Pubmed: 1846850
  • Yura, T., Mori, H., Nagai, H., Nagata, T., Ishihama, A., Fujita, N., Isono, K., Mizobuchi, K., Nakata, A. (1992). "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Nucleic Acids Res 20:3305-3308. Pubmed: 1630901