Identification |
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Name: | Penicillin-binding protein 1A |
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Synonyms: | - PBP-1a
- PBP1a
- Penicillin-insensitive transglycosylase
- Peptidoglycan TGase
- Penicillin-sensitive transpeptidase
- DD-transpeptidase
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Gene Name: | mrcA |
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Enzyme Class: | Not Available |
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Biological Properties |
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General Function: | Involved in catalytic activity |
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Specific Function: | Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits) |
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Cellular Location: | Cell inner membrane; Single-pass type II membrane protein |
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SMPDB Pathways: | |
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KEGG Pathways: | |
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SMPDB Reactions: | |
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Complex Reactions: | |
1.0 | + | 1.0two linked disacharide pentapeptide murein units (uncrosslinked, middle of chain) | → | 1.0 | + | 1.0 | + | 1.0three linked disacharide pentapeptide murein units (uncrosslinked, middle of chain) |
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2.0 | → | 2.0 | + | 2.0 | + | 1.0two linked disacharide pentapeptide murein units (uncrosslinked, middle of chain) |
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1.0two linked disacharide pentapeptide murein units (uncrosslinked, middle of chain) | → | 1.0 | + | 1.0two disacharide linked murein units, pentapeptide crosslinked tetrapeptide (A2pm->D-ala) (middle of chain) |
| 1.0two linked disacharide pentapeptide murein units (uncrosslinked, middle of chain) → 1.0 D-Alanine + 1.0two disacharide linked murein units, pentapeptide crosslinked tetrapeptide (A2pm->D-ala) (middle of chain) ReactionCard | |
1.0three linked disacharide pentapeptide murein units (uncrosslinked, middle of chain) | → | 2.0 | + | 1.0three disacharide linked murein units (pentapeptide crosslinked tetrapeptide (A2pm->D-ala) tetrapeptide corsslinked tetrapeptide (A2pm->D-ala)) (middle of chain) |
| 1.0three linked disacharide pentapeptide murein units (uncrosslinked, middle of chain) → 2.0 D-Alanine + 1.0three disacharide linked murein units (pentapeptide crosslinked tetrapeptide (A2pm->D-ala) tetrapeptide corsslinked tetrapeptide (A2pm->D-ala)) (middle of chain) ReactionCard | |
1.0two linked disacharide pentapeptide murein units (uncrosslinked, middle of chain) | → | 1.0 | + | 1.0two disacharide linked murein units, pentapeptide corsslinked tripeptide (A2pm->A2pm) (middle of chain) |
| 1.0two linked disacharide pentapeptide murein units (uncrosslinked, middle of chain) → 1.0 D-Alanyl-D-alanine + 1.0two disacharide linked murein units, pentapeptide corsslinked tripeptide (A2pm->A2pm) (middle of chain) ReactionCard |
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Metabolites: | ECMDB ID | Name | View |
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ECMDB01310 | D-Alanine | MetaboCard | ECMDB03459 | D-Alanyl-D-alanine | MetaboCard | ECMDB21225 | Hydrogen ion | MetaboCard | ECMDB23023 | lipid II(A) | MetaboCard | ECMDB01469 | Undecaprenyl diphosphate | MetaboCard | ECMDB20210 | Undecaprenyl-diphospho-N-acetylmuramoyl-(N-acetylglucosamine)-L-alanyl-D-glutaminyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine | MetaboCard | ECMDB20212 | Undecaprenyl-diphospho-N-acetylmuramoyl-(N-acetylglucosamine)-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine | MetaboCard |
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GO Classification: | Component |
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cell part | cell wall | external encapsulating structure | peptidoglycan-based cell wall | Function |
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binding | catalytic activity | drug binding | hydrolase activity | penicillin binding | peptidase activity | transferase activity | transferase activity, transferring glycosyl groups | transferase activity, transferring pentosyl groups | Process |
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aminoglycan metabolic process | carbohydrate metabolic process | cell wall biogenesis | cell wall organization or biogenesis | cellular cell wall organization or biogenesis | cellular component organization or biogenesis | glycosaminoglycan metabolic process | metabolic process | peptidoglycan biosynthetic process | peptidoglycan metabolic process | peptidoglycan-based cell wall biogenesis | polysaccharide metabolic process | primary metabolic process | response to antibiotic | response to chemical stimulus | response to stimulus |
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Gene Properties |
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Blattner: | b3396 |
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Gene Orientation | Clockwise |
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Centisome Percentage: | 75.89 |
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Left Sequence End | 3520893 |
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Right Sequence End | 3523445 |
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Gene Sequence: | >2553 bp
GTGAAGTTCGTAAAGTATTTTTTGATCCTTGCAGTCTGTTGCATTCTGCTGGGAGCAGGC
TCGATTTATGGCCTATACCGCTACATCGAGCCACAACTGCCGGATGTGGCGACATTAAAA
GATGTTCGCCTGCAAATTCCGATGCAGATTTACAGCGCCGATGGCGAGCTGATTGCTCAA
TACGGTGAGAAACGTCGTATTCCGGTTACGTTGGATCAAATCCCACCGGAGATGGTGAAA
GCCTTTATCGCGACAGAAGACAGCCGCTTCTACGAGCATCACGGCGTTGACCCGGTGGGG
ATCTTCCGTGCAGCAAGCGTGGCGCTGTTCTCCGGTCACGCGTCACAAGGGGCAAGTACC
ATTACCCAGCAGCTGGCGAGAAACTTCTTCCTCAGTCCAGAACGCACGCTGATGCGTAAG
ATTAAGGAAGTCTTCCTCGCGATTCGCATTGAACAGCTGCTGACGAAAGACGAGATCCTC
GAGCTTTATCTGAACAAGATTTACCTTGGTTACCGCGCCTATGGTGTCGGTGCTGCGGCA
CAAGTCTATTTCGGAAAAACGGTCGACCAACTGACGCTGAACGAAATGGCGGTGATAGCC
GGGCTGCCGAAAGCGCCTTCCACCTTCAACCCGCTCTACTCGATGGATCGTGCCGTCGCG
CGGCGTAACGTCGTGCTGTCGCGGATGCTGGATGAAGGGTATATCACCCAACAACAGTTC
GATCAGACACGCACTGAGGCGATTAACGCTAACTATCACGCGCCGGAGATTGCTTTCTCT
GCGCCGTACCTGAGCGAAATGGTGCGCCAGGAGATGTATAACCGTTATGGCGAAAGTGCC
TATGAAGACGGTTATCGCATTTACACCACCATCACCCGCAAAGTGCAGCAGGCCGCGCAG
CAGGCGGTACGTAATAACGTGCTGGACTACGACATGCGCCACGGCTATCGCGGCCCGGCA
AATGTGCTGTGGAAAGTGGGCGAGTCGGCGTGGGATAACAACAAGATTACCGATACGCTG
AAGGCGCTGCCAACCTATGGTCCGCTGCTGCCTGCCGCAGTCACCAGCGCCAATCCTCAG
CAAGCGACGGCGATGCTGGCGGACGGGTCGACCGTCGCATTGAGTATGGAAGGCGTTCGC
TGGGCGCGTCCTTACCGTTCGGATACTCAGCAAGGACCGACGCCGCGTAAAGTGACCGAT
GTTCTGCAAACGGGTCAGCAAATCTGGGTTCGTCAGGTTGGCGATGCATGGTGGCTGGCA
CAAGTGCCGGAAGTGAACTCGGCGCTGGTGTCGATCAATCCGCAAAACGGTGCCGTTATG
GCGCTGGTCGGTGGCTTTGATTTCAATCAGAGCAAGTTTAACCGCGCCACCCAGGCACTG
CGTCAGGTGGGTTCCAACATCAAACCGTTCCTCTACACCGCGGCGATGGATAAAGGTCTG
ACGCTGGCAAGTATGTTGAACGATGTGCCAATTTCTCGCTGGGATGCAAGTGCCGGTTCT
GACTGGCAGCCGAAGAACTCACCACCGCAGTATGCTGGTCCAATTCGCTTACGTCAGGGG
CTGGGTCAGTCGAAAAACGTGGTGATGGTACGCGCAATGCGGGCGATGGGCGTCGACTAC
GCTGCAGAATATCTGCAACGCTTCGGCTTCCCGGCACAAAACATTGTCCACACCGAATCG
CTGGCGCTGGGTTCAGCGTCCTTCACCCCAATGCAGGTGGCGCGCGGCTACGCGGTCATG
GCGAACGGCGGCTTCCTGGTGGACCCGTGGTTTATCAGCAAAATTGAAAACGATCAGGGC
GGCGTGATTTTCGAAGCGAAACCGAAAGTAGCCTGCCCGGAATGCGATATTCCGGTGATT
TACGGTGATACGCAGAAATCGAACGTGCTGGAAAATAACGATGTTGAAGATGTCGCTATC
TCCCGCGAGCAGCAGAATGTTTCTGTACCAATGCCGCAGCTGGAGCAGGCAAATCAGGCG
TTAGTGGCGAAGACTGGCGCGCAGGAGTACGCACCGCACGTCATCAACACTCCGCTGGCA
TTCCTGATTAAGAGTGCTTTGAACACCAATATCTTTGGTGAGCCAGGCTGGCAGGGTACT
GGCTGGCGTGCAGGTCGTGATTTGCAGCGTCGCGATATCGGCGGGAAAACCGGGACCACT
AACAGTTCGAAAGATGCGTGGTTCTCGGGTTACGGTCCGGGCGTTGTGACCTCGGTCTGG
ATTGGCTTTGATGATCACCGTCGTAATCTCGGTCATACAACGGCTTCCGGAGCGATTAAA
GATCAGATCTCAGGTTACGAAGGCGGTGCCAAGAGTGCCCAGCCTGCATGGGACGCTTAT
ATGAAAGCCGTTCTTGAAGGTGTGCCGGAGCAGCCGCTGACGCCGCCACCGGGTATTGTG
ACGGTGAATATCGATCGCAGCACCGGGCAGTTAGCTAATGGTGGCAACAGCCGCGAAGAG
TATTTCATCGAAGGTACGCAGCCGACACAACAGGCAGTGCACGAGGTGGGAACGACCATT
ATCGATAATGGCGAGGCACAGGAATTGTTCTGA |
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Protein Properties |
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Pfam Domain Function: | |
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Protein Residues: | 850 |
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Protein Molecular Weight: | 93636 |
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Protein Theoretical pI: | 7 |
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Signaling Regions: | |
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Transmembrane Regions: | |
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Protein Sequence: | >Penicillin-binding protein 1A
MKFVKYFLILAVCCILLGAGSIYGLYRYIEPQLPDVATLKDVRLQIPMQIYSADGELIAQ
YGEKRRIPVTLDQIPPEMVKAFIATEDSRFYEHHGVDPVGIFRAASVALFSGHASQGAST
ITQQLARNFFLSPERTLMRKIKEVFLAIRIEQLLTKDEILELYLNKIYLGYRAYGVGAAA
QVYFGKTVDQLTLNEMAVIAGLPKAPSTFNPLYSMDRAVARRNVVLSRMLDEGYITQQQF
DQTRTEAINANYHAPEIAFSAPYLSEMVRQEMYNRYGESAYEDGYRIYTTITRKVQQAAQ
QAVRNNVLDYDMRHGYRGPANVLWKVGESAWDNNKITDTLKALPTYGPLLPAAVTSANPQ
QATAMLADGSTVALSMEGVRWARPYRSDTQQGPTPRKVTDVLQTGQQIWVRQVGDAWWLA
QVPEVNSALVSINPQNGAVMALVGGFDFNQSKFNRATQALRQVGSNIKPFLYTAAMDKGL
TLASMLNDVPISRWDASAGSDWQPKNSPPQYAGPIRLRQGLGQSKNVVMVRAMRAMGVDY
AAEYLQRFGFPAQNIVHTESLALGSASFTPMQVARGYAVMANGGFLVDPWFISKIENDQG
GVIFEAKPKVACPECDIPVIYGDTQKSNVLENNDVEDVAISREQQNVSVPMPQLEQANQA
LVAKTGAQEYAPHVINTPLAFLIKSALNTNIFGEPGWQGTGWRAGRDLQRRDIGGKTGTT
NSSKDAWFSGYGPGVVTSVWIGFDDHRRNLGHTTASGAIKDQISGYEGGAKSAQPAWDAY
MKAVLEGVPEQPLTPPPGIVTVNIDRSTGQLANGGNSREEYFIEGTQPTQQAVHEVGTTI
IDNGEAQELF |
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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
- Broome-Smith, J. K., Edelman, A., Yousif, S., Spratt, B. G. (1985). "The nucleotide sequences of the ponA and ponB genes encoding penicillin-binding protein 1A and 1B of Escherichia coli K12." Eur J Biochem 147:437-446. Pubmed: 3882429
- Goffin, C., Ghuysen, J. M. (1998). "Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs." Microbiol Mol Biol Rev 62:1079-1093. Pubmed: 9841666
- 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
- Ishino, F., Mitsui, K., Tamaki, S., Matsuhashi, M. (1980). "Dual enzyme activities of cell wall peptidoglycan synthesis, peptidoglycan transglycosylase and penicillin-sensitive transpeptidase, in purified preparations of Escherichia coli penicillin-binding protein 1A." Biochem Biophys Res Commun 97:287-293. Pubmed: 7006606
- Keck, W., Glauner, B., Schwarz, U., Broome-Smith, J. K., Spratt, B. G. (1985). "Sequences of the active-site peptides of three of the high-Mr penicillin-binding proteins of Escherichia coli K-12." Proc Natl Acad Sci U S A 82:1999-2003. Pubmed: 3920658
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