| 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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