User:Pakpoom Subsoontorn/Notebook/Shape Determination in Bacteria/2008/10/26

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Enzymes(genes) involving in building E.coli cell wall

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List

  • AmiA
  • AmiC
  • AmpC
  • AmpH
  • FtsA
  • FtsBL
  • FtsK
  • FtsQ
  • FtsW
  • FtsZ
  • MepA(mepA)
  • MinC
  • MinD
  • MinE
  • MreB
  • MreC
  • MreD
  • PBP1a(ponA)
  • PBP1B(ponB)
  • PBP1c(pbpC)
  • PBP2(pbpA)
  • PBP3(pbpB or ftsI)
  • PBP4(dacB)
  • PBP5(dacA)
  • PBP6(dacC)
  • PBP6b(dacD)
  • PBP7(pbpG)
  • RodA
  • ZipA

Detail

  • AmiA
    • Class: Alanine amidases
    • Function: degrade cell wall cross like at the septum by cleaving peptide moiety from the MurNAc so contribute to daughter cell separation(1-73, 1-82)
    • Localization: AmiA-GFP was found to be dispersed throughout the periplasm of the cells
  • AmiC
    • Class: Alanine amidases
    • Function: degrade cell wall cross like at the septum by cleaving peptide moiety from the MurNAc so contribute to daughter cell separation
    • Localization: AmiA-GFP was found to be dispersed throughout the periplasm of the small cells but localized almost exclusively at the septal ring of the constricting cells (1-10)
  • AmpC(1-76)
    • Class: beta-lactamase
    • Function: Affect cell shape (1-76)
  • AmpH(1-76)
    • Class: beta-lactamase
    • Function: Affect cell shape (1-76)
  • MepA(1-92)
    • Class: LMW endopeptidase
    • Function: Penicillin-insensitive endopeptidase
  • MreB
    • Function: possibly actin homolog. absence in spherical bacterium. require for rod shape formation in E.coli. Depletion of MreBCD can be suppressed by over expression FtsQAZ (1-98).
  • MreC
    • Function: function with MreB, essential for rod shape formation in E.coli.Depletion of MreBCD can be suppressed by over expression FtsQAZ(1-98).
  • MreD
    • Function: function with MreB, essetial for rod shape formation in E.coli.Depletion of MreBCD can be suppressed by over expression FtsQAZ(1-98).
  • PBP1a(1-19)
    • Function: transglycosylation, transpeptidation (1)
  • PBP1b(1-19)
    • Function: transglycosylation, transpeptidation (1)
  • PBP1c(1-172)
    • Function: transglycosylation; binds to PBPs1B, -2, -3 and MltA (1-172)
  • PBP2
    • Function: elongation-specific TPase (1-183). Exhibit a preference for pentapeptide side-chain (1-148). Possibly help maintaining the diameter of the cell as PBP2 inhibitor, amdinocillin (mecillinam) induces the increment of pole diameter at newly formed cell poles (1-36)
    • Localization: Spot-like pattern along lateral membrane, division site (GFP)(1-36)
  • PBP3 (1-127)
    • Function: cell-division specific TPase (1-183). N-terminal domain is required for folding and stability of penicillin binding module, functioning as an intramolecular chaperone (1-64). Exhibit a preference for tripeptide chain (1-16)
    • Localization: division septum (IF, GFP)(1-200, 1-205). Have some interaction with cell division protein FtsZ,-A,-Q,-L,-W (1-118, 1-204)
  • PBP4 (1-97)
    • Class: LMW endopeptidase
    • Function: control of cell shape, together with PBP5 (1-117)
  • PBP5 (1-20)
    • Class: LMW carboxypeptidase
    • Function: control of cell shape (1-117, 1-129, 1-130). Stain with defective PBP5 has high frequency for branching (1-42)
  • PBP6 (1-20)
    • Class: LMW carboxypeptidase
  • PBP6b (1-7)
    • Class: LMW carboxypeptidase
  • PBP7 (1-75)
    • Class: LMW endopeptidase
    • Function: control of cell shape, together with PBP5 (1-117)
  • RodA (1-78)
    • Class: translocase or flipase
    • Function: possibly transport lipid-linked precursor of PG through cell wall outside. The mutant rodA(Ts) grows as sphere(1-78).Depletion effect can be suppressed by over expression FtsQAZ (1-194).

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Reference

  1. Scheffers, DJ and Pinho, MG. Bacterial Cell Wall Synthesis: New Insight from Localization Studies. Microbiology and Molecular biology review, Dec. 2005, p585-607


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