Identification
Name:Penicillin-binding protein 1A
Synonyms:
  • PBP-1a
  • PBP1a
  • Penicillin-insensitive transglycosylase
  • Peptidoglycan TGase
  • Penicillin-sensitive transpeptidase
  • DD-transpeptidase
Gene Name:mrcA
Enzyme Class:Not Available
Biological Properties
General Function:Involved in catalytic activity
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)
Cellular Location:Cell inner membrane; Single-pass type II membrane protein
SMPDB Pathways:
KEGG Pathways:
SMPDB Reactions:
2.0Thumb1.0Thumb+1.0Thumb+1.0 a peptidoglycan dimer (meso-diaminopimelate containing)
2.0lipid II(A) → 1.0Undecaprenyl diphosphate + 1.0Hydrogen ion + 1.0 a peptidoglycan dimer (meso-diaminopimelate containing)
ReactionCard
1.0 a peptidoglycan dimer (meso-diaminopimelate containing)1.0Thumb+1.0a peptidoglycan with D,D cross-links (meso-diaminopimelate containing)
1.0 a peptidoglycan dimer (meso-diaminopimelate containing) → 1.0D-Alanine + 1.0a peptidoglycan with D,D cross-links (meso-diaminopimelate containing)
ReactionCard
2.0Thumb1.0 a peptidoglycan dimer (meso-diaminopimelate containing)+1.0Thumb+1.0Thumb
Complex Reactions:
1.0Thumb+1.0two linked disacharide pentapeptide murein units (uncrosslinked, middle of chain)1.0Thumb+1.0Thumb+1.0three linked disacharide pentapeptide murein units (uncrosslinked, middle of chain)
1.0Undecaprenyl-diphospho-N-acetylmuramoyl-(N-acetylglucosamine)-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + 1.0two linked disacharide pentapeptide murein units (uncrosslinked, middle of chain) → 1.0Hydrogen ion + 1.0Undecaprenyl diphosphate + 1.0three linked disacharide pentapeptide murein units (uncrosslinked, middle of chain)
ReactionCard
2.0Thumb2.0Thumb+2.0Thumb+1.0two linked disacharide pentapeptide murein units (uncrosslinked, middle of chain)
1.0two linked disacharide pentapeptide murein units (uncrosslinked, middle of chain)1.0Thumb+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) → 1.0D-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)2.0Thumb+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) → 2.0D-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)1.0Thumb+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) → 1.0D-Alanyl-D-alanine + 1.0two disacharide linked murein units, pentapeptide corsslinked tripeptide (A2pm->A2pm) (middle of chain)
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01310D-AlanineMetaboCard
ECMDB03459D-Alanyl-D-alanineMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB23023lipid II(A)MetaboCard
ECMDB01469Undecaprenyl diphosphateMetaboCard
ECMDB20210Undecaprenyl-diphospho-N-acetylmuramoyl-(N-acetylglucosamine)-L-alanyl-D-glutaminyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanineMetaboCard
ECMDB20212Undecaprenyl-diphospho-N-acetylmuramoyl-(N-acetylglucosamine)-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanineMetaboCard
GO Classification:
Component
cell part
cell wall
external encapsulating structure
peptidoglycan-based cell wall
Function
binding
catalytic activity
drug binding
hydrolase activity
penicillin binding
peptidase activity
transferase activity
transferase activity, transferring glycosyl groups
transferase activity, transferring pentosyl groups
Process
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
Gene Properties
Blattner:b3396
Gene OrientationClockwise
Centisome Percentage:75.89
Left Sequence End3520893
Right Sequence End3523445
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
Protein Properties
Pfam Domain Function:
Protein Residues:850
Protein Molecular Weight:93636
Protein Theoretical pI:7
Signaling Regions:
  • None
Transmembrane Regions:
  • 6-26
Protein Sequence:
>Penicillin-binding protein 1A
MKFVKYFLILAVCCILLGAGSIYGLYRYIEPQLPDVATLKDVRLQIPMQIYSADGELIAQ
YGEKRRIPVTLDQIPPEMVKAFIATEDSRFYEHHGVDPVGIFRAASVALFSGHASQGAST
ITQQLARNFFLSPERTLMRKIKEVFLAIRIEQLLTKDEILELYLNKIYLGYRAYGVGAAA
QVYFGKTVDQLTLNEMAVIAGLPKAPSTFNPLYSMDRAVARRNVVLSRMLDEGYITQQQF
DQTRTEAINANYHAPEIAFSAPYLSEMVRQEMYNRYGESAYEDGYRIYTTITRKVQQAAQ
QAVRNNVLDYDMRHGYRGPANVLWKVGESAWDNNKITDTLKALPTYGPLLPAAVTSANPQ
QATAMLADGSTVALSMEGVRWARPYRSDTQQGPTPRKVTDVLQTGQQIWVRQVGDAWWLA
QVPEVNSALVSINPQNGAVMALVGGFDFNQSKFNRATQALRQVGSNIKPFLYTAAMDKGL
TLASMLNDVPISRWDASAGSDWQPKNSPPQYAGPIRLRQGLGQSKNVVMVRAMRAMGVDY
AAEYLQRFGFPAQNIVHTESLALGSASFTPMQVARGYAVMANGGFLVDPWFISKIENDQG
GVIFEAKPKVACPECDIPVIYGDTQKSNVLENNDVEDVAISREQQNVSVPMPQLEQANQA
LVAKTGAQEYAPHVINTPLAFLIKSALNTNIFGEPGWQGTGWRAGRDLQRRDIGGKTGTT
NSSKDAWFSGYGPGVVTSVWIGFDDHRRNLGHTTASGAIKDQISGYEGGAKSAQPAWDAY
MKAVLEGVPEQPLTPPPGIVTVNIDRSTGQLANGGNSREEYFIEGTQPTQQAVHEVGTTI
IDNGEAQELF
References
External Links:
ResourceLink
Uniprot ID:P02918
Uniprot Name:PBPA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85676645
Ecogene ID:EG10748
Ecocyc:EG10748
ColiBase:b3396
Kegg Gene:b3396
EchoBASE ID:EB0741
CCDB:PBPA_ECOLI
BacMap:162135911
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