Penicillin-binding protein 1B (P02919)

Identification
Name:Penicillin-binding protein 1B
Synonyms:
  • PBP-1b
  • PBP1b
  • Murein polymerase
  • Penicillin-insensitive transglycosylase
  • Peptidoglycan TGase
  • Peptidoglycan glycosyltransferase
  • Penicillin-sensitive transpeptidase
  • DD-transpeptidase
Gene Name:mrcB
Enzyme Class:
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:
KEGG Reactions:
1.0Thumb+1.0[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-g-D-Glu-A2pm-D-Ala-D-Ala)]n-diphosphoundecaprenol ↔ 1.0di-trans,poly-cis-Undecaprenyl diphosphate+1.0[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-g-D-Glu-A2pm-D-Ala-D-Ala)]n-diphosphoundecaprenol
1.0Undecaprenyl-diphospho-N-acetylmuramoyl-(N-acetylglucosamine)-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + 1.0[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-g-D-Glu-A2pm-D-Ala-D-Ala)]n-diphosphoundecaprenol ↔ 1.0di-trans,poly-cis-Undecaprenyl diphosphate + 1.0[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-g-D-Glu-A2pm-D-Ala-D-Ala)]n-diphosphoundecaprenol
ReactionCard
1.0[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-g-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol+1.0Thumb ↔ 1.0Thumb
1.0[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-g-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + 1.0Undecaprenyl-diphospho-N-acetylmuramoyl-(N-acetylglucosamine)-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine ↔ 1.0Undecaprenyl diphosphate
ReactionCard
SMPDB Reactions:
2.0Thumb → 1.0Thumb+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
2.0Thumb → 1.0 a peptidoglycan dimer (meso-diaminopimelate containing)+1.0Thumb+1.0Thumb
2.0Undecaprenyl-diphospho-N-acetylmuramoyl-(N-acetylglucosamine)-L-alanyl-D-glutaminyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine → 1.0 a peptidoglycan dimer (meso-diaminopimelate containing) + 1.0Undecaprenyl diphosphate + 1.0Hydrogen ion
ReactionCard
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
2.0Thumb → 2.0Thumb+2.0Thumb+1.0two linked disacharide pentapeptide murein units (uncrosslinked, middle of chain)
2.0Undecaprenyl-diphospho-N-acetylmuramoyl-(N-acetylglucosamine)-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine → 2.0Hydrogen ion + 2.0Undecaprenyl diphosphate + 1.0two linked disacharide pentapeptide murein units (uncrosslinked, middle of chain)
ReactionCard
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
1.0(GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n)-diphosphoundecaprenol+1.0Thumb → 1.0(GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol+1.0Thumb
1.0(GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n)-diphosphoundecaprenol + 1.0GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol → 1.0(GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + 1.0Undecaprenyl diphosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01310D-AlanineMetaboCard
ECMDB03459D-Alanyl-D-alanineMetaboCard
ECMDB23024GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenolMetaboCard
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
peptidoglycan glycosyltransferase activity
transferase activity
transferase activity, transferring glycosyl groups
transferase activity, transferring hexosyl 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:b0149
Gene OrientationClockwise
Centisome Percentage:3.55
Left Sequence End164730
Right Sequence End167264
Gene Sequence:
>2535 bp
ATGGCCGGGAATGACCGCGAGCCAATTGGACGCAAAGGGAAACCGACGCGTCCGGTCAAA
CAAAAGGTAAGCCGTCGTCGTTACGAAGATGACGATGATTACGACGATTATGATGACTAT
GAGGATGAAGAACCGATGCCGCGCAAAGGTAAGGGCAAAGGCAAAGGGCGTAAGCCTCGT
GGCAAACGCGGCTGGCTATGGCTACTGCTAAAACTGGCTATCGTTTTTGCCGTGCTGATC
GCCATTTACGGCGTTTATCTCGATCAAAAAATTCGTAGCCGTATTGATGGCAAGGTCTGG
CAACTGCCTGCGGCAGTTTATGGCCGAATGGTCAATCTTGAGCCAGACATGACCATCAGC
AAGAACGAGATGGTGAAGCTGCTGGAGGCGACCCAGTATCGTCAGGTGTCGAAAATGACC
CGTCCTGGCGAATTTACCGTGCAGGCCAACAGCATTGAGATGATTCGCCGTCCGTTTGAT
TTCCCGGACAGTAAAGAAGGACAGGTGCGCGCGCGTCTGACCTTTGATGGCGATCATCTG
GCGACGATCGTCAATATGGAGAACAACCGTCAGTTCGGTTTCTTCCGTCTTGATCCGCGT
CTGATCACCATGATCTCTTCGCCAAACGGTGAGCAGCGTCTGTTTGTGCCGCGCAGTGGT
TTCCCGGATTTGCTGGTGGATACTTTGCTGGCGACAGAAGACCGTCATTTTTACGAGCAT
GATGGAATCAGTCTCTACTCAATCGGACGTGCGGTGCTGGCAAACCTGACCGCCGGACGC
ACGGTACAGGGTGCGAGTACGCTGACGCAACAGCTGGTGAAAAACCTGTTCCTCTCCAGC
GAGCGTTCTTACTGGCGTAAAGCGAACGAAGCTTACATGGCGCTGATCATGGACGCGCGT
TACAGCAAAGACCGTATTCTTGAGCTGTATATGAACGAGGTGTATCTCGGTCAGAGCGGC
GACAACGAAATCCGCGGCTTCCCGCTGGCAAGCTTGTATTACTTTGGTCGCCCGGTAGAA
GAGCTAAGCCTCGACCAGCAGGCGCTGTTAGTCGGTATGGTGAAAGGGGCGTCCATCTAC
AACCCGTGGCGTAACCCAAAACTGGCGCTGGAGCGACGTAATCTGGTGCTGCGTCTGCTG
CAACAGCAACAGATTATTGATCAAGAACTCTATGACATGTTGAGTGCCCGTCCGCTGGGG
GTTCAGCCGCGCGGTGGGGTGATCTCTCCTCAGCCAGCCTTTATGCAACTGGTGCGTCAG
GAGCTGCAGGCAAAACTGGGCGATAAGGTAAAAGATCTCTCCGGCGTGAAGATCTTCACT
ACCTTTGACTCGGTGGCCCAGGACGCGGCAGAAAAAGCCGCCGTGGAAGGCATTCCGGCA
CTGAAGAAACAGCGTAAGTTGAGCGATCTTGAAACTGCGATTGTGGTCGTCGACCGCTTT
AGTGGTGAAGTTCGTGCGATGGTCGGAGGTTCTGAGCCGCAGTTTGCGGGCTACAACCGT
GCGATGCAGGCGCGTCGTTCGATTGGTTCCCTTGCAAAACCAGCGACTTATCTGACGGCC
TTAAGCCAGCCGAAAATCTATCGTCTGAATACGTGGATTGCGGATGCGCCAATTGCGCTG
CGTCAGCCGAATGGCCAGGTCTGGTCACCGCAGAATGATGACCGTCGTTATAGCGAAAGC
GGCAGAGTGATGCTGGTGGATGCGTTGACCCGTTCGATGAACGTGCCGACGGTAAATCTG
GGGATGGCGCTGGGGCTGCCTGCGGTTACGGAGACCTGGATTAAACTGGGCGTACCGAAA
GATCAGTTGCATCCGGTTCCGGCAATGCTGCTGGGGGCGTTGAACTTAACGCCAATCGAA
GTGGCGCAGGCATTCCAGACCATCGCCAGCGGTGGTAACCGTGCACCGCTTTCTGCGCTG
CGTTCGGTAATCGCGGAAGATGGCAAAGTGCTGTATCAGAGCTTCCCGCAGGCGGAACGC
GCTGTTCCGGCGCAGGCGGCGTATCTGACACTATGGACCATGCAGCAGGTGGTACAACGC
GGTACGGGTCGTCAGCTTGGGGCGAAATACCCGAACCTGCATCTGGCAGGGAAAACAGGG
ACTACCAACAATAACGTAGATACCTGGTTTGCGGGCATTGACGGCAGCACGGTGACCATC
ACCTGGGTCGGCCGTGATAACAACCAGCCGACCAAACTGTATGGTGCCAGCGGGGCAATG
TCGATTTATCAGCGTTATCTGGCTAACCAGACGCCAACGCCGCTGAATCTTGTTCCGCCA
GAAGATATTGCAGATATGGGCGTGGACTACGACGGCAACTTTGTTTGCAGCGGTGGCATG
CGTATCTTGCCGGTCTGGACCAGCGATCCGCAATCGCTGTGCCAGCAGAGCGAGATGCAG
CAGCAGCCGTCAGGCAATCCGTTTGATCAGTCTTCTCAGCCGCAGCAACAGCCGCAACAG
CAACCTGCTCAGCAAGAGCAGAAAGACAGCGACGGTGTAGCCGGTTGGATCAAGGATATG
TTTGGTAGTAATTAA
Protein Properties
Pfam Domain Function:
Protein Residues:844
Protein Molecular Weight:94292
Protein Theoretical pI:9
Signaling Regions:
  • None
Transmembrane Regions:
  • 64-87
Protein Sequence:
>Penicillin-binding protein 1B
MAGNDREPIGRKGKPTRPVKQKVSRRRYEDDDDYDDYDDYEDEEPMPRKGKGKGKGRKPR
GKRGWLWLLLKLAIVFAVLIAIYGVYLDQKIRSRIDGKVWQLPAAVYGRMVNLEPDMTIS
KNEMVKLLEATQYRQVSKMTRPGEFTVQANSIEMIRRPFDFPDSKEGQVRARLTFDGDHL
ATIVNMENNRQFGFFRLDPRLITMISSPNGEQRLFVPRSGFPDLLVDTLLATEDRHFYEH
DGISLYSIGRAVLANLTAGRTVQGASTLTQQLVKNLFLSSERSYWRKANEAYMALIMDAR
YSKDRILELYMNEVYLGQSGDNEIRGFPLASLYYFGRPVEELSLDQQALLVGMVKGASIY
NPWRNPKLALERRNLVLRLLQQQQIIDQELYDMLSARPLGVQPRGGVISPQPAFMQLVRQ
ELQAKLGDKVKDLSGVKIFTTFDSVAQDAAEKAAVEGIPALKKQRKLSDLETAIVVVDRF
SGEVRAMVGGSEPQFAGYNRAMQARRSIGSLAKPATYLTALSQPKIYRLNTWIADAPIAL
RQPNGQVWSPQNDDRRYSESGRVMLVDALTRSMNVPTVNLGMALGLPAVTETWIKLGVPK
DQLHPVPAMLLGALNLTPIEVAQAFQTIASGGNRAPLSALRSVIAEDGKVLYQSFPQAER
AVPAQAAYLTLWTMQQVVQRGTGRQLGAKYPNLHLAGKTGTTNNNVDTWFAGIDGSTVTI
TWVGRDNNQPTKLYGASGAMSIYQRYLANQTPTPLNLVPPEDIADMGVDYDGNFVCSGGM
RILPVWTSDPQSLCQQSEMQQQPSGNPFDQSSQPQQQPQQQPAQQEQKDSDGVAGWIKDM
FGSN
References
External Links:
ResourceLink
Uniprot ID:P02919
Uniprot Name:PBPB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674355
Ecogene ID:EG10605
Ecocyc:EG10605
ColiBase:b0149
Kegg Gene:b0149
EchoBASE ID:EB0600
CCDB:PBPB_ECOLI
BacMap:16128142
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
  • Edelman, A., Bowler, L., Broome-Smith, J. K., Spratt, B. G. (1987). "Use of a beta-lactamase fusion vector to investigate the organization of penicillin-binding protein 1B in the cytoplasmic membrane of Escherichia coli." Mol Microbiol 1:101-106. Pubmed: 3330753
  • Fujita, N., Mori, H., Yura, T., Ishihama, A. (1994). "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Nucleic Acids Res 22:1637-1639. Pubmed: 8202364
  • 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
  • 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
  • Lefevre, F., Remy, M. H., Masson, J. M. (1997). "Topographical and functional investigation of Escherichia coli penicillin-binding protein 1b by alanine stretch scanning mutagenesis." J Bacteriol 179:4761-4767. Pubmed: 9244263
  • Sung, M. T., Lai, Y. T., Huang, C. Y., Chou, L. Y., Shih, H. W., Cheng, W. C., Wong, C. H., Ma, C. (2009). "Crystal structure of the membrane-bound bifunctional transglycosylase PBP1b from Escherichia coli." Proc Natl Acad Sci U S A 106:8824-8829. Pubmed: 19458048
  • Terrak, M., Ghosh, T. K., van Heijenoort, J., Van Beeumen, J., Lampilas, M., Aszodi, J., Ayala, J. A., Ghuysen, J. M., Nguyen-Disteche, M. (1999). "The catalytic, glycosyl transferase and acyl transferase modules of the cell wall peptidoglycan-polymerizing penicillin-binding protein 1b of Escherichia coli." Mol Microbiol 34:350-364. Pubmed: 10564478
  • 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
  • Wang, C. C., Schultz, D. E., Nicholas, R. A. (1996). "Localization of a putative second membrane association site in penicillin-binding protein 1B of Escherichia coli." Biochem J 316 ( Pt 1):149-156. Pubmed: 8645198
  • Zijderveld, C. A., Aarsman, M. E., den Blaauwen, T., Nanninga, N. (1991). "Penicillin-binding protein 1B of Escherichia coli exists in dimeric forms." J Bacteriol 173:5740-5746. Pubmed: 1885547