Family Search for PF06295 (ZapG-like)

PF06295 hits 17 sequences in PaperBLAST's database above the trusted cutoff. Showing hits to curated sequences only. Or see all hits or try another family.

YhcB / b3233 DUF1043 domain-containing inner membrane protein YhcB from Escherichia coli K-12 substr. MG1655 (see 8 papers)
ZAPG_ECOLI / P0ADW3 Z-ring associated protein G; Cell division protein ZapG; LPS assembly protein LapD from Escherichia coli (strain K12) (see 8 papers)
Aligns to 6:127 / 132 (92.4%), covers 99.2% of PF06295, 165.9 bits

• function: Involved in cell division, cell envelope biogenesis and cell shape maintenance (PubMed:27335665, PubMed:32323199, PubMed:33895137, PubMed:34941903). Is a key regulator of cell envelope growth, playing a crucial role in coordinating cell width, elongation and division to maintain cell envelope integrity (PubMed:34941903). Plays an important role in the lipopolysaccharide (LPS) assembly/transport (PubMed:36077106). It may regulate LpxC levels and assist MsbA-mediated LPS transport (PubMed:36077106).
  subunit: Forms homooligomers (PubMed:21210718). Interacts with proteins of the divisome, such as FtsI and FtsQ, and of the elongasome, such as RodZ and RodA (PubMed:27335665, PubMed:33895137). Also interacts several other proteins, including the shape-determining proteins MreC and MreD, the N-acetylglucosaminyl transferase MurG and the lipopolysaccharide assembly protein LapA (PubMed:27335665). It also copurifies with LapB and various proteins involved in LPS biosynthesis/transport and phospholipid biosynthesis (PubMed:36077106).
  disruption phenotype: Deletion of the gene results in morphological aberration, such as branched shape, and cell division defects, such as filamentous growth, defects in DNA segregation and generation of chromosome-less cells (PubMed:32323199, PubMed:33895137). It also shows abnormal FtsZ ring formation and aberrant septum development (PubMed:33895137). Deletion causes high sensitivities to various envelope stresses, loss of envelope stability, increased membrane permeability and causes growth defect under normal growth conditions (PubMed:32323199, PubMed:34941903). Loss of the gene results in aberrant cell size driven by the production of excess membrane phospholipids (PubMed:34941903). The knockout mutant does not grow at 45 degrees Celsius and is hypersensitive to cell wall-acting antibiotics, even in the stationary phase (PubMed:33895137). Mutant is highly susceptible to vancomycin and various anti-folate antibiotics such as such as trimethoprim, sulfanilamide and sulfamethazine (PubMed:32323199). Loss of the gene causes a reduction in LpxC amounts and LPS defects (PubMed:36077106). The deletion of both zapG and rodZ genes causes synthetic lethality (PubMed:27335665, PubMed:34941903). Deletion is also synthetically lethal with components of peptidoglycan synthesis and recycling pathways (PubMed:34941903). No change in function or assembly of the cytochrome bd-I complex (PubMed:16863643).

ZAPG_HAEDU / Q7VLF5 Z-ring associated protein G; Cell division protein ZapG from Haemophilus ducreyi (strain 35000HP / ATCC 700724) (see paper)
Aligns to 12:128 / 128 (91.4%), covers 98.4% of PF06295, 117.3 bits

• function: Involved in cell division, cell envelope biogenesis and cell shape maintenance.
  subunit: Homotetramer (PubMed:33895137). In solution, is primarily monomeric but forms small amounts of stable tetramer and hexadecamer (PubMed:33895137). The crystal structure of the cytosolic region shows a coiled-coil tetramer in the asymmetric unit that is very likely to be a physiologically relevant assembly of the protein (PubMed:33895137).

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