Identification |
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Name: | Membrane-bound lytic murein transglycosylase A |
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Synonyms: | |
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Gene Name: | mltA |
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Enzyme Class: | Not Available |
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Biological Properties |
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General Function: | Involved in hydrolase activity, hydrolyzing O-glycosyl compounds |
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Specific Function: | Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. Degrades murein glycan strands and insoluble, high-molecular weight murein sacculi |
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Cellular Location: | Cell outer membrane; Lipid-anchor |
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SMPDB Pathways: | Not Available |
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KEGG Pathways: | Not Available |
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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 |
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Complex Reactions: | |
1.0two linked disacharide tetrapeptide and tripeptide murein units (uncrosslinked, middle of chain) | → | 1.0 | + | 1.0 |
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1.0two linked disacharide tripeptide murein units (uncrosslinked, middle of chain) | → | 2.0 |
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1.0two linked disacharide tetrapeptide murein units (uncrosslinked, middle of chain) | → | 2.0 |
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1.0three disacharide linked murein units (tetrapeptide crosslinked tetrapeptide (A2pm->D-ala), one uncrosslinked tetrapaptide) (middle of chain) | → | 1.0 | + | 1.0two disacharide linked murein units, tetrapeptide corsslinked tetrapeptide (A2pm->D-ala) (middle of chain) |
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Metabolites: | ECMDB ID | Name | View |
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ECMDB21249 | N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tetrapeptide | MetaboCard | ECMDB21250 | N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tripeptide | MetaboCard |
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GO Classification: | Component |
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cell part | membrane | outer membrane | Function |
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catalytic activity | hydrolase activity | hydrolase activity, acting on glycosyl bonds | hydrolase activity, hydrolyzing O-glycosyl compounds | Process |
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aminoglycan metabolic process | carbohydrate metabolic process | glycosaminoglycan metabolic process | metabolic process | peptidoglycan metabolic process | peptidoglycan turnover | polysaccharide metabolic process | primary metabolic process |
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Gene Properties |
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Blattner: | b2813 |
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Gene Orientation | Counterclockwise |
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Centisome Percentage: | 63.45 |
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Left Sequence End | 2944103 |
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Right Sequence End | 2945200 |
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Gene Sequence: | >1098 bp
GTGATTAAATTTCTCTCTGCATTAATTCTTCTACTGGTCACGACGGCGGCTCAGGCTGAG
CGTATTCGCGATCTCACCAGTGTTCAGGGGGTAAGGCAAAACTCACTGATTGGCTATGGT
CTGGTGGTGGGGCTGGATGGCACCGGTGACCAGACAACCCAGACGCCGTTTACCACACAA
ACGCTTAATAACATGCTCTCACAGCTGGGAATTACCGTTCCGACGGGCACCAATATGCAG
CTAAAAAACGTCGCTGCGGTAATGGTGACAGCGTCACTTCCTCCGTTTGGACGTCAGGGG
CAAACCATCGATGTGGTGGTTTCTTCCATGGGAAATGCCAAAAGCTTGCGTGGAGGTACG
TTGTTGATGACACCGCTTAAGGGCGTTGACAGTCAGGTGTATGCGCTGGCGCAGGGCAAT
ATTCTGGTTGGCGGCGCAGGAGCCTCCGCTGGCGGTAGCAGTGTTCAGGTTAACCAACTG
AACGGTGGACGGATCACCAATGGTGCGGTTATTGAACGTGAATTGCCCAGCCAGTTTGGC
GTCGGGAATACCCTTAATTTGCAACTTAACGACGAAGATTTCAGCATGGCGCAGCAAATC
GCTGACACCATCAACCGCGTGCGTGGATATGGCAGCGCCACCGCGTTAGATGCGCGGACT
ATTCAGGTGCGCGTACCGAGTGGCAACAGTTCCCAGGTCCGCTTCCTTGCCGATATTCAG
AATATGCAGGTTAATGTCACCCCGCAGGACGCTAAAGTAGTGATTAACTCGCGCACCGGT
TCGGTGGTGATGAATCGCGAAGTGACCCTCGACAGCTGCGCGGTAGCGCAGGGGAATCTC
TCAGTAACAGTTAATCGTCAGGCCAATGTCAGCCAGCCAGATACACCGTTTGGTGGTGGA
CAGACTGTGGTTACTCCACAAACGCAGATCGATTTACGCCAGAGCGGCGGTTCGCTGCAA
AGCGTACGTTCCAGCGCCAGCCTCAATAACGTGGTGCGCGCGCTCAATGCGCTGGGCGCT
ACGCCGATGGATCTGATGTCCATACTGCAATCAATGCAAAGTGCGGGATGTCTGCGGGCA
AAACTGGAAATCATCTGA |
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Protein Properties |
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Pfam Domain Function: | |
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Protein Residues: | 365 |
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Protein Molecular Weight: | 40410 |
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Protein Theoretical pI: | 9 |
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Signaling Regions: | |
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Transmembrane Regions: | |
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Protein Sequence: | >Membrane-bound lytic murein transglycosylase A
MKGRWVKYLLMGTVVAMLAACSSKPTDRGQQYKDGKFTQPFSLVNQPDAVGAPINAGDFA
EQINHIRNSSPRLYGNQSNVYNAVQEWLRAGGDTRNMRQFGIDAWQMEGADNYGNVQFTG
YYTPVIQARHTRQGEFQYPIYRMPPKRGRLPSRAEIYAGALSDKYILAYSNSLMDNFIMD
VQGSGYIDFGDGSPLNFFSYAGKNGHAYRSIGKVLIDRGEVKKEDMSMQAIRHWGETHSE
AEVRELLEQNPSFVFFKPQSFAPVKGASAVPLVGRASVASDRSIIPPGTTLLAEVPLLDN
NGKFNGQYELRLMVALDVGGAIKGQHFDIYQGIGPEAGHRAGWYNHYGRVWVLKTAPGAG
NVFSG |
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References |
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External Links: | |
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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
- Lommatzsch, J., Templin, M. F., Kraft, A. R., Vollmer, W., Holtje, J. V. (1997). "Outer membrane localization of murein hydrolases: MltA, a third lipoprotein lytic transglycosylase in Escherichia coli." J Bacteriol 179:5465-5470. Pubmed: 9287002
- Ursinus, A., Holtje, J. V. (1994). "Purification and properties of a membrane-bound lytic transglycosylase from Escherichia coli." J Bacteriol 176:338-343. Pubmed: 8288527
- Vollmer, W., von Rechenberg, M., Holtje, J. V. (1999). "Demonstration of molecular interactions between the murein polymerase PBP1B, the lytic transglycosylase MltA, and the scaffolding protein MipA of Escherichia coli." J Biol Chem 274:6726-6734. Pubmed: 10037771
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