Membrane-bound lytic murein transglycosylase B (P41052)

Identification
Name:Membrane-bound lytic murein transglycosylase B
Synonyms:
  • 35 kDa soluble lytic transglycosylase
  • Murein hydrolase B
  • Slt35
Gene Name:mltB
Enzyme Class:Not Available
Biological Properties
General Function:Cell wall/membrane/envelope biogenesis
Specific Function:Murein-degrading enzyme. Catalyzes the cleavage of the glycosidic bonds between N-acetylmuramic acid and N- acetylglucosamine residues in peptidoglycan. May play a role in recycling of muropeptides during cell elongation and/or cell division
Cellular Location:Cell outer membrane; Lipid-anchor; Periplasmic side
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:Not Available
Gene Properties
Blattner:b2701
Gene OrientationCounterclockwise
Centisome Percentage:60.83
Left Sequence End2822513
Right Sequence End2823598
Gene Sequence:
>1086 bp
ATGGAAAGTGGTCATCGCTTTGATGCTCAGACGCTGCACAGTTTTATTCAGGCTGTATTT
CGTCAGATGGGTAGCGAGGAACAAGAAGCGAAATTAGTTGCCGATCATTTAATCGCGGCA
AACCTGGCAGGGCATGATTCACATGGTATTGGCATGATCCCAAGCTATGTACGCTCCTGG
AGTCAGGGGCACCTGCAAATTAACCATCATGCCAAAACCGTTAAAGAGGCGGGGGCGGCG
GTCACGCTCGATGGCGATCGCGCATTTGGTCAGGTCGCGGCACATGAAGCGATGGCGCTG
GGGATTGAGAAAGCGCATCAGCACGGTATTGCCGCCGTGGCGCTACATAACTCGCATCAT
ATCGGCCGTATCGGTTACTGGGCGGAGCAGTGTGCAGCGGCGGGGTTTGTCTCTATCCAC
TTTGTTAGCGTGGTCGGTATTCCAATGGTCGCGCCGTTCCACGGTCGCGACAGCCGCTTT
GGCACCAATCCGTTCTGTGTGGTTTTCCCTCGTAAAGATAATTTCCCGCTGTTGCTTGAT
TACGCCACCAGCGCCATTGCATTTGGCAAAACCCGCGTCGCCTGGCATAAAGGCGTCCCC
GTGCCGCCAGGTTGCCTGATTGACGTTAACGGCGTGCCGACGACCAATCCGGCGGTAATG
CAGGAGTCGCCGTTGGGTTCGCTGTTGACCTTTGCCGAACATAAAGGCTACGCCCTTGCA
GCGATGTGTGAAATTCTTGGCGGGGCGCTTTCCGGCGGTAAAACGACGCATCAGGAAACG
TTACAAACCAGTCCCGATGCCATTCTTAACTGCATGACCACTATCATCATCAACCCGGAA
CTCTTCGGCGCGCCGGATTGTAACGCGCAGACCGAAGCCTTTGCCGAGTGGGTGAAAGCC
TCGCCGCATGATGATGATAAGCCGATTTTGCTACCGGGCGAGTGGGAAGTGAACACGCGT
CGCGAACGGCAGAAGCAGGGGATTCCACTGGATGCGGGAAGCTGGCAGGCCATTTGTGAT
GCAGCGCGGCAGATTGGTATGCCGGAAGAGACGTTGCAGGCTTTCTGTCAGCAGTTAGCC
AGCTAA
Protein Properties
Pfam Domain Function:Not Available
Protein Residues:361
Protein Molecular Weight:40256
Protein Theoretical pI:9
PDB File:1D0L
Signaling Regions:
  • 1-18
Transmembrane Regions:
  • None
Protein Sequence:
>Membrane-bound lytic murein transglycosylase B
MFKRRYVTLLPLFVLLAACSSKPKPTETDTTTGTPSGGFLLEPQHNVMQMGGDFANNPNA
QQFIDKMVNKHGFDRQQLQEILSQAKRLDSVLRLMDNQAPTTSVKPPSGPNGAWLRYRKK
FITPDNVQNGVVFWNQYEDALNRAWQVYGVPPEIIVGIIGVETRWGRVMGKTRILDALAT
LSFNYPRRAEYFSGELETFLLMARDEQDDPLNLKGSFAGAMGYGQFMPSSYKQYAVDFSG
DGHINLWDPVDAIGSVANYFKAHGWVKGDQVAVMANGQAPGLPNGFKTKYSISQLAAAGL
TPQQPLGNHQQASLLRLDVGTGYQYWYGLPNFYTITRYNHSTHYAMAVWQLGQAVALARV
Q
References
External Links:
ResourceLink
Uniprot ID:P41052
Uniprot Name:MLTB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062362
PDB ID:1D0L
Ecogene ID:EG12699
Ecocyc:EG12699
ColiBase:b2701
Kegg Gene:b2701
EchoBASE ID:EB2561
CCDB:MLTB_ECOLI
BacMap:16130608
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
  • Dijkstra, A. J., Hermann, F., Keck, W. (1995). "Cloning and controlled overexpression of the gene encoding the 35 kDa soluble lytic transglycosylase from Escherichia coli." FEBS Lett 366:115-118. Pubmed: 7789526
  • Ehlert, K., Holtje, J. V., Templin, M. F. (1995). "Cloning and expression of a murein hydrolase lipoprotein from Escherichia coli." Mol Microbiol 16:761-768. Pubmed: 7476170
  • 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
  • van Asselt, E. J., Dijkstra, A. J., Kalk, K. H., Takacs, B., Keck, W., Dijkstra, B. W. (1999). "Crystal structure of Escherichia coli lytic transglycosylase Slt35 reveals a lysozyme-like catalytic domain with an EF-hand." Structure 7:1167-1180. Pubmed: 10545329
  • van Asselt, E. J., Dijkstra, B. W. (1999). "Binding of calcium in the EF-hand of Escherichia coli lytic transglycosylase Slt35 is important for stability." FEBS Lett 458:429-435. Pubmed: 10570954
  • van Asselt, E. J., Kalk, K. H., Dijkstra, B. W. (2000). "Crystallographic studies of the interactions of Escherichia coli lytic transglycosylase Slt35 with peptidoglycan." Biochemistry 39:1924-1934. Pubmed: 10684641
  • Van Asselt, E. J., Perrakis, A., Kalk, K. H., Lamzin, V. S., Dijkstra, B. W. (1998). "Accelerated X-ray structure elucidation of a 36 kDa muramidase/transglycosylase using wARP." Acta Crystallogr D Biol Crystallogr 54:58-73. Pubmed: 9761817
  • Yamada, M., Saier, M. H. Jr (1987). "Glucitol-specific enzymes of the phosphotransferase system in Escherichia coli. Nucleotide sequence of the gut operon." J Biol Chem 262:5455-5463. Pubmed: 3553176
  • Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837