Family Search for PF06295 (DUF1043)

PF06295 hits 16 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, 166.8 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, 136.3 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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