Membrane-bound lytic murein transglycosylase F (P0AGC5)

Identification
Name:Membrane-bound lytic murein transglycosylase F
Synonyms:
  • Murein lyase F
Gene Name:mltF
Enzyme Class:Not Available
Biological Properties
General Function:Involved in carbon-oxygen lyase activity, acting on polysaccharides
Specific Function:Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella
Cellular Location:Cell outer membrane; Peripheral membrane protein.
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
EcoCyc Reactions:
1.0a peptidoglycan polymer ? 1.0a peptidoglycan polymer with 1,6-anhydromuropeptide end+1.0a peptidoglycan polymer with GlcNAc end
1.0a peptidoglycan polymer ? 1.0a peptidoglycan polymer with 1,6-anhydromuropeptide end + 1.0a peptidoglycan polymer with GlcNAc end
ReactionCard
Complex Reactions:
1.0two linked disacharide tetrapeptide and tripeptide murein units (uncrosslinked, middle of chain) → 1.0Thumb+1.0Thumb
1.0two linked disacharide tetrapeptide and tripeptide murein units (uncrosslinked, middle of chain) → 1.0N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tripeptide + 1.0N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tetrapeptide
ReactionCard
1.0two linked disacharide tripeptide murein units (uncrosslinked, middle of chain) → 2.0Thumb
1.0two linked disacharide tripeptide murein units (uncrosslinked, middle of chain) → 2.0N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tripeptide
ReactionCard
1.0two linked disacharide tetrapeptide murein units (uncrosslinked, middle of chain) → 2.0Thumb
1.0two linked disacharide tetrapeptide murein units (uncrosslinked, middle of chain) → 2.0N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tetrapeptide
ReactionCard
1.0three disacharide linked murein units (tetrapeptide crosslinked tetrapeptide (A2pm->D-ala), one uncrosslinked tetrapaptide) (middle of chain) → 1.0Thumb+1.0two disacharide linked murein units, tetrapeptide corsslinked tetrapeptide (A2pm->D-ala) (middle of chain)
1.0three disacharide linked murein units (tetrapeptide crosslinked tetrapeptide (A2pm->D-ala), one uncrosslinked tetrapaptide) (middle of chain) → 1.0N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tetrapeptide + 1.0two disacharide linked murein units, tetrapeptide corsslinked tetrapeptide (A2pm->D-ala) (middle of chain)
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB21249N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tetrapeptideMetaboCard
ECMDB21250N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tripeptideMetaboCard
GO Classification:
Component
cell part
membrane
outer membrane-bounded periplasmic space
periplasmic space
Function
catalytic activity
lytic transglycosylase activity
transferase activity
transferase activity, transferring glycosyl groups
transporter activity
Process
aminoglycan metabolic process
carbohydrate metabolic process
establishment of localization
glycosaminoglycan metabolic process
metabolic process
peptidoglycan metabolic process
polysaccharide metabolic process
primary metabolic process
transport
Gene Properties
Blattner:b2558
Gene OrientationClockwise
Centisome Percentage:58.06
Left Sequence End2693823
Right Sequence End2695379
Gene Sequence:
>1557 bp
ATGTTCATACGCGCTCCCAATTTTGGACGTAAGCTCCTGCTTACCTGCATTGTTGCAGGC
GTAATGATTGCGATACTGGTGAGTTGCCTTCAGTTTTTAGTGGCCTGGCATAAGCACGAA
GTCAAATACGACACACTGATTACCGACGTACAAAAGTATCTCGATACCTATTTTGCCGAC
CTGAAATCCACTACTGACCGGCTCCAGCCGCTGACCTTAGATACCTGCCAGCAAGCTAAC
CCCGAACTGACCGCCCGCGCAGCGTTTAGCATGAATGTCCGAACGTTTGTGCTGGTGAAA
GATAAAAAAACATTCTGTTCATCTGCGACCGGTGAGATGGACATTCCACTCAATGAATTG
ATTCCGGCGCTCGACATTAATAAAAACGTCGATATGGCGATCTTACCCGGCACGCCGATG
GTGCCGAACAAACCCGCAATCGTCATCTGGTATCGCAACCCTTTGCTGAAAAATAGCGGC
GTCTTTGCCGCTCTGAATCTCAACCTGACGCCTTCACTCTTTTATAGTTCACGGCAGGAA
GATTACGATGGCGTCGCCCTCATTATTGGCAATACTGCGCTATCTACCTTTTCTTCACGT
TTGATGAACGTTAACGAATTAACCGACATGCCAGTCCGTGAAACTAAAATTGCGGGCATT
CCTCTGACCGTTCGGCTTTATGCAGATGACTGGACATGGAACGATGTGTGGTACGCATTT
TTACTGGGCGGCATGAGTGGAACTGTCGTTGGCCTGCTCTGCTATTACCTGATGAGCGTA
CGTATGCGCCCCGGCAGAGAAATCATGACCGCCATCAAGCGCGAACAATTTTACGTGGCG
TATCAACCGGTGGTGGATACACAAGCTTTGCGAGTAACGGGCCTGGAAGTACTGCTACGC
TGGCGGCATCCTGTCGCGGGAGAAATTCCCCCGGATGCCTTCATTAACTTTGCCGAATCG
CAAAAGATGATTGTGCCGCTGACTCAGCACCTGTTTGAGTTAATTGCCCGCGATGCCGCA
GAATTAGAAAAAGTGCTGCCGGTAGGCGTCAAATTTGGTATTAACATTGCGCCGGACCAT
CTGCACAGCGAAAGCTTTAAAGCAGATATCCAGAAACTGCTCACTTCCCTGCCCGCACAC
CATTTCCAGATTGTGCTGGAAATTACCGAGCGCGATATGTTGAAAGAGCAAGAAGCCACA
CAACTCTTCGCCTGGCTGCACTCGGTCGGCGTAGAAATTGCTATTGATGACTTCGGCACC
GGGCACAGCGCGCTTATCTATCTTGAGCGTTTTACGCTCGATTATCTGAAAATTGACCGT
GGATTTATCAACGCCATCGGTACGGAAACGATCACTTCCCCCGTACTTGACGCGGTGCTG
ACGCTGGCGAAACGCCTCAATATGCTGACGGTTGCTGAAGGGGTCGAAACGCCGGAACAG
GCGCGATGGCTAAGCGAACGCGGCGTTAATTTCATGCAAGGCTACTGGATTAGCCGCCCG
TTACCGCTGGACGATTTTGTTCGCTGGCTAAAGAAACCGTATACGCCGCAGTGGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:518
Protein Molecular Weight:58302
Protein Theoretical pI:5
Signaling Regions:
  • 1-21
Transmembrane Regions:
  • None
Protein Sequence:
>Membrane-bound lytic murein transglycosylase F
MKKLKINYLFIGILALLLAVALWPSIPWFGKADNRIAAIQARGELRVSTIHTPLTYNEIN
GKPFGLDYELAKQFADYLGVKLKVTVRQNISQLFDDLDNGNADLLAAGLVYNSERVKNYQ
PGPTYYSVSQQLVYKVGQYRPRTLGNLTAEQLTVAPGHVVVNDLQTLKETKFPELSWKVD
DKKGSAELMEDVIEGKLDYTIADSVAISLFQRVHPELAVALDITDEQPVTWFSPLDGDNT
LSAALLDFFNEMNEDGTLARIEEKYLGHGDDFDYVDTRTFLRAVDAVLPQLKPLFEKYAE
EIDWRLLAAIAYQESHWDAQATSPTGVRGMMMLTKNTAQSLGITDRTDAEQSISGGVRYL
QDMMSKVPESVPENERIWFALAAYNMGYAHMLDARALTAKTKGNPDSWADVKQRLPLLSQ
KPYYSKLTYGYARGHEAYAYVENIRKYQISLVGYLQEKEKQATEAAMQLAQDYPAVSPTE
LGKEKFPFLSFLSQSSSNYLTHSPSLLFSRKGSEEKQN
References
External Links:
ResourceLink
Uniprot ID:P0AGC5
Uniprot Name:MLTF_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1736841
Ecogene ID:EG11373
Ecocyc:EG11373
ColiBase:b2558
Kegg Gene:b2558
EchoBASE ID:EB1347
CCDB:MLTF_ECOLI
BacMap:171701683
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
  • 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
  • Koonin, E. V., Rudd, K. E. (1994). "A conserved domain in putative bacterial and bacteriophage transglycosylases." Trends Biochem Sci 19:106-107. Pubmed: 8203016
  • Poulsen, L. K., Larsen, N. W., Molin, S., Andersson, P. (1992). "Analysis of an Escherichia coli mutant strain resistant to the cell-killing function encoded by the gef gene family." Mol Microbiol 6:895-905. Pubmed: 1602968
  • Schendel, F. J., Mueller, E., Stubbe, J., Shiau, A., Smith, J. M. (1989). "Formylglycinamide ribonucleotide synthetase from Escherichia coli: cloning, sequencing, overproduction, isolation, and characterization." Biochemistry 28:2459-2471. Pubmed: 2659070
  • Scheurwater, E. M., Clarke, A. J. (2008). "The C-terminal domain of Escherichia coli YfhD functions as a lytic transglycosylase." J Biol Chem 283:8363-8373. Pubmed: 18234673
  • Scheurwater, E., Reid, C. W., Clarke, A. J. (2008). "Lytic transglycosylases: bacterial space-making autolysins." Int J Biochem Cell Biol 40:586-591. Pubmed: 17468031