Soluble lytic murein transglycosylase (P0AGC3)

Identification
Name:Soluble lytic murein transglycosylase
Synonyms:
  • Exomuramidase
  • Peptidoglycan lytic exotransglycosylase
  • Slt70
Gene Name:slt
Enzyme Class:Not Available
Biological Properties
General Function:Involved in hydrolase activity, hydrolyzing O-glycosyl compounds
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:Periplasm.
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
periplasmic space
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on glycosyl bonds
hydrolase activity, hydrolyzing O-glycosyl compounds
lytic transglycosylase activity
transferase activity
transferase activity, transferring glycosyl groups
Process
aminoglycan metabolic process
carbohydrate metabolic process
glycosaminoglycan metabolic process
metabolic process
peptidoglycan metabolic process
polysaccharide metabolic process
primary metabolic process
Gene Properties
Blattner:b4392
Gene OrientationClockwise
Centisome Percentage:99.76
Left Sequence End4628756
Right Sequence End4630693
Gene Sequence:
>1938 bp
GTGGAAAAAGCCAAACAAGTTACCTGGCGGCTGTTGGCTGCCGGTGTCTGTCTGCTGACG
GTCAGCAGCGTGGCGCGAGCCGACTCACTGGATGAGCAGCGTAGTCGTTACGCGCAAATC
AAGCAGGCCTGGGATAATCGACAAATGGATGTGGTCGAACAAATGATGCCTGGACTGAAG
GATTATCCGCTTTATCCCTACCTGGAATACCGCCAGATCACCGATGATCTGATGAATCAA
CCGGCGGTGACGGTCACTAACTTTGTTCGCGCTAACCCCACGCTTCCTCCCGCTCGCACG
CTGCAATCTCGTTTCGTCAATGAACTGGCGCGGCGTGAAGACTGGCGTGGCTTGTTAGCC
TTTAGCCCGGAAAAGCCCGGAACTACCGAAGCGCAATGTAATTACTACTATGCGAAATGG
AACACCGGGCAGAGTGAAGAAGCCTGGCAAGGGGCGAAAGAGCTGTGGCTAACCGGCAAG
AGCCAGCCTAACGCCTGTGACAAGTTATTTAGCGTCTGGCGTGCGTCAGGTAAACAAGAT
CCGCTGGCGTATTTAGAGCGTATCCGTCTGGCGATGAAAGCGGGTAACACAGGCCTGGTA
ACAGTGCTGGCAGGGCAGATGCCTGCCGATTACCAGACTATCGCCTCGGCAATCATTTCA
CTGGCGAACAACCCTAATACGGTACTGACCTTCGCGCGTACAACTGGCGCGACCGATTTT
ACCCGTCAAATGGCGGCGGTGGCGTTTGCCAGTGTGGCGCGGCAGGATGCTGAGAATGCA
CGGCTGATGATCCCATCGCTTGCCCAGGCGCAGCAGCTTAATGAAGATCAGATTCAGGAG
CTGCGCGATATCGTCGCCTGGCGTTTGATGGGCAACGATGTCACCGACGAGCAGGCGAAA
TGGCGCGATGACGCCATTATGCGCTCGCAATCTACTTCGCTTATTGAACGCCGTGTACGA
ATGGCGCTTGGCACCGGCGATCGTCGCGGCCTGAATACCTGGCTGGCGCGTCTGCCTATG
GAAGCGAAAGAGAAAGATGAATGGCGTTACTGGCAGGCGGATTTATTGCTGGAACGCGGA
CGTGAAGCTGAAGCAAAAGAGATTTTGCATCAACTCATGCAACAGCGTGGTTTCTACCCG
ATGGTTGCAGCACAACGCATCGGCGAAGAGTATGAGCTGAAGATTGATAAAGCGCCGCAG
AATGTTGACAGCGCCCTGACTCAGGGGCCGGAGATGGCGCGCGTGCGCGAGTTGATGTAC
TGGAATCTCGATAATACCGCGCGTAGCGAGTGGGCCAATCTGGTGAAGAGCAAGTCAAAA
ACAGAGCAGGCTCAACTGGCGCGGTATGCTTTCAACAACCAATGGTGGGATCTTAGCGTT
CAGGCAACGATCGCCGGGAAGCTGTGGGATCATCTGGAAGAGCGATTCCCGCTGGCTTAC
AACGATCTTTTCAAACGCTACACCAGCGGTAAGGAGATCCCGCAAAGCTATGCGATGGCG
ATTGCTCGTCAGGAGAGCGCCTGGAATCCGAAAGTGAAATCACCGGTAGGGGCCAGCGGC
TTGATGCAGATTATGCCTGGTACAGCGACCCATACGGTGAAGATGTTCTCTATTCCCGGT
TATAGCAGTCCTGGGCAATTGCTGGATCCGGAAACGAATATCAACATTGGCACCAGTTAC
CTGCAATATGTTTATCAGCAGTTTGGCAATAATCGTATTTTCTCCTCAGCAGCTTATAAC
GCCGGACCAGGGCGGGTGCGAACCTGGCTTGGCAACAGCGCCGGGCGTATCGACGCAGTG
GCATTTGTCGAGAGTATTCCATTCTCCGAGACGCGCGGTTATGTGAAGAACGTGCTGGCT
TATGACGCTTACTACCGCTATTTCATGGGGGATAAACCGACGTTGATGAGCGCCACGGAA
TGGGGACGTCGTTACTGA
Protein Properties
Pfam Domain Function:
Protein Residues:645
Protein Molecular Weight:73353
Protein Theoretical pI:9
PDB File:1QSA
Signaling Regions:
  • 1-27
Transmembrane Regions:
  • None
Protein Sequence:
>Soluble lytic murein transglycosylase
MEKAKQVTWRLLAAGVCLLTVSSVARADSLDEQRSRYAQIKQAWDNRQMDVVEQMMPGLK
DYPLYPYLEYRQITDDLMNQPAVTVTNFVRANPTLPPARTLQSRFVNELARREDWRGLLA
FSPEKPGTTEAQCNYYYAKWNTGQSEEAWQGAKELWLTGKSQPNACDKLFSVWRASGKQD
PLAYLERIRLAMKAGNTGLVTVLAGQMPADYQTIASAIISLANNPNTVLTFARTTGATDF
TRQMAAVAFASVARQDAENARLMIPSLAQAQQLNEDQIQELRDIVAWRLMGNDVTDEQAK
WRDDAIMRSQSTSLIERRVRMALGTGDRRGLNTWLARLPMEAKEKDEWRYWQADLLLERG
REAEAKEILHQLMQQRGFYPMVAAQRIGEEYELKIDKAPQNVDSALTQGPEMARVRELMY
WNLDNTARSEWANLVKSKSKTEQAQLARYAFNNQWWDLSVQATIAGKLWDHLEERFPLAY
NDLFKRYTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMFSIPG
YSSPGQLLDPETNINIGTSYLQYVYQQFGNNRIFSSAAYNAGPGRVRTWLGNSAGRIDAV
AFVESIPFSETRGYVKNVLAYDAYYRYFMGDKPTLMSATEWGRRY
References
External Links:
ResourceLink
Uniprot ID:P0AGC3
Uniprot Name:SLT_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85677131
PDB ID:1QSA
Ecogene ID:EG10950
Ecocyc:EG10950
ColiBase:b4392
Kegg Gene:b4392
EchoBASE ID:EB0943
CCDB:SLT_ECOLI
BacMap:90111747
General Reference:
  • Betzner, A. S., Keck, W. (1989). "Molecular cloning, overexpression and mapping of the slt gene encoding the soluble lytic transglycosylase of Escherichia coli." Mol Gen Genet 219:489-491. Pubmed: 2695826
  • 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
  • Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L., Blattner, F. R. (1995). "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Nucleic Acids Res 23:2105-2119. Pubmed: 7610040
  • Engel, H., Kazemier, B., Keck, W. (1991). "Murein-metabolizing enzymes from Escherichia coli: sequence analysis and controlled overexpression of the slt gene, which encodes the soluble lytic transglycosylase." J Bacteriol 173:6773-6782. Pubmed: 1938883
  • Gunsalus, R. P., Yanofsky, C. (1980). "Nucleotide sequence and expression of Escherichia coli trpR, the structural gene for the trp aporepressor." Proc Natl Acad Sci U S A 77:7117-7121. Pubmed: 7012834
  • 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
  • Rozeboom, H. J., Dijkstra, B. W., Engel, H., Keck, W. (1990). "Crystallization of the soluble lytic transglycosylase from Escherichia coli K12." J Mol Biol 212:557-559. Pubmed: 2184239
  • Singleton, C. K., Roeder, W. D., Bogosian, G., Somerville, R. L., Weith, H. L. (1980). "DNA sequence of the E. coli trpR gene and prediction of the amino acid sequence of Trp repressor." Nucleic Acids Res 8:1551-1560. Pubmed: 7001368
  • Thunnissen, A. M., Dijkstra, A. J., Kalk, K. H., Rozeboom, H. J., Engel, H., Keck, W., Dijkstra, B. W. (1994). "Doughnut-shaped structure of a bacterial muramidase revealed by X-ray crystallography." Nature 367:750-753. Pubmed: 8107871
  • Thunnissen, A. M., Rozeboom, H. J., Kalk, K. H., Dijkstra, B. W. (1995). "Structure of the 70-kDa soluble lytic transglycosylase complexed with bulgecin A. Implications for the enzymatic mechanism." Biochemistry 34:12729-12737. Pubmed: 7548026
  • van Asselt, E. J., Thunnissen, A. M., Dijkstra, B. W. (1999). "High resolution crystal structures of the Escherichia coli lytic transglycosylase Slt70 and its complex with a peptidoglycan fragment." J Mol Biol 291:877-898. Pubmed: 10452894