Family Search for PF13355 (ARC6-like_IMS)

April 2024: GapMind for amino acid biosynthesis has been updated to include newly-discovered enzymes and comparative genomics predictions (see details)

Running HMMer for PF13355

PF13355 hits 7 sequences in PaperBLAST's database above the trusted cutoff. Showing hits to curated sequences only. Or see all hits or try another family.

ARC6_ARATH / Q9FIG9 Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 6, chloroplastic; AtARC6 from Arabidopsis thaliana (Mouse-ear cress) (see 24 papers)
Aligns to 679:794 / 801 (14.5%), covers 100.0% of PF13355, 106.3 bits

• function: Component of the plastid division machinery consisting in a binary fission accomplished by the simultaneous constriction of the FtsZ ring on the stromal side of the inner envelope membrane, and the ARC5 ring on the cytosolic side of the outer envelope membrane (PubMed:28248291, PubMed:29466386). Involved in the initiation of proplastid and plastid division (including chloroplasts, statoliths and leukoplasts) (PubMed:29466386). Promotes the assembly and/or stabilization of the plastid-dividing FtsZ ring, functioning as an antagonistic regulator of FtsZ dynamics against CDP1 and facilitating MCD1 positioning to membrane tethered FtsZ filaments to form the chloroplast Z-Ring; inhibits GDP-induced disassembly of FTSZ2 but enables ARC3 binding to FTSZ2-1 (PubMed:29466386, PubMed:29967285, PubMed:29769312, PubMed:29138260). Relays plastid division site position between stroma and outer surface via interactions with the stromal FtsZ ring and the outer membrane PDV2 that recruits cytoplasmic ARC5 ring (PubMed:28248291). Required for plastid equatorial positioning of PDV2 and ARC5. May contribute to gravitropism in stems and hypocotyls. Seems to influence stromule (stroma-filled tubular extensions of the plastid envelope membrane) length and frequency.
  subunit: Self-interacts (PubMed:28248291, PubMed:29769312). Part of a complex made of ARC3, ARC6, FTSZ1 and FTSZ2 (PubMed:22823492). Interacts with FTSZ2-1 and FTSZ2-2 (via C-terminus), but not with FTSZ1; this interaction enables ARC3 binding to FTSZ2 (PubMed:29967285, PubMed:29769312, PubMed:29138260, PubMed:26527658). Binds to CDT1A. Interacts (via C-terminus) with PDV2 (via C-terminus) in the chloroplast intermembrane space; this interaction induces homodimerization and leads to the formation of an heterotetramer containing two ARC6 and two PDV2 subunits (PubMed:28248291). Interacts with MCD1 in the chloroplast stroma and facilitates its subsequent binding to FtsZ2-1 (PubMed:29967285). Interacts (via J domain) with CJD1 (via J-like domain) (PubMed:22028775).
  disruption phenotype: Defective in proplastid and plastid division, with only one or two grossly enlarged plastids per cell, sometimes exhibiting alteration in stromule length and frequency in non-green tissues (e.g. increase in the frequency of stromules in nearly all cells) and in stomatal guard cells (GCs) (PubMed:29466386). Heterogeneous chloroplasts sizes and shapes such as giant and mini- plastids in leaf epidermal pavement cells (PCs) (PubMed:29466386). Abnormal subplastidial localization of the key plastid division proteins FTSZ1 and FTSZ2 (numerous short and disorganized FtsZ filament fragments) (PubMed:29967285). Root cells statoliths, chloroplasts, and other plastids are also abnormally large. Impaired gravitropism of inflorescence stems and hypocotyls, but not of roots. Several mesophyll and stomatal guard cells contain chlorophyll-free plastids, probably missing chloroplastic DNA. Misexpression and mislocalization of ADT2 (PubMed:30252596). The double mutant mcd1 arc6 exhibits similar chloroplast defect than the single mutant arc6, including the abnormal localization of FTSZ1 to short filaments and dots within chloroplasts (PubMed:29967285). The double mutant arc6 cjd1 exhibits both phenotypes of single mutants cjd1 and arc6 including altered fatty acid profiles and heterogeneous chloroplasts sizes and shapes, respectively (PubMed:22028775).

CDP1_ARATH / Q8VY16 Plastid division protein CDP1, chloroplastic; ARC6-homolog protein; Protein CHLOROPLAST DIVISION SITE POSITIONING 1; AtCDP1; Protein PARALOG OF ARC6; Protein STROMULE BIOGENESIS ALTERED 2 from Arabidopsis thaliana (Mouse-ear cress) (see 6 papers)
Aligns to 693:811 / 819 (14.5%), covers 99.1% of PF13355, 101.6 bits

• function: Component of the plastid division machinery required for PDV1 localization to constriction sites. Involved in chloroplast division site placement (PubMed:28984364, PubMed:23936263). Required for the proper formation of FtsZ rings at the division site in nongreen plastids (e.g. etioplasts) (PubMed:23936263). Inhibits FtsZ assembly, functioning as an antagonistic regulator of FtsZ dynamics against ARC6, by recruiting ARC3 to the middle of the plastid to facilitates its interaction with FtsZ proteins (PubMed:26527658, PubMed:30824505). Required during stromule biogenesis in the leaf epidermis, especially in non-mesophyll cells plastids (PubMed:28984364).
  subunit: Self-interacts (PubMed:19564892, PubMed:28984364). Interacts (via N-terminus) with ARC3 (via MORN domains) (PubMed:19453460, PubMed:19564892, PubMed:26527658). Binds (via N-terminus) to FTSZ2 proteins, FTSZ2-1 and FTSZ2-2 (PubMed:26527658, PubMed:28984364, PubMed:30824505). Recruited ARC3 to the middle of the plastid where subsequent complex made of CDP1/PARC6, ARC3 and FtsZ proteins can form; this complex enhances the dynamics of Z rings during chloroplast division (PubMed:30824505). Interacts (via C-terminus) with PDV1 (via C-terminus) (PubMed:26527658). Interacts with MIND1 (PubMed:28984364).
  disruption phenotype: Defects of chloroplast and FtsZ filament morphology (e.g. long FtsZ filaments formed by multiple rings or spirals); elongated chloroplasts with multiple division sites (PubMed:19453460, PubMed:19564892, PubMed:23936263). Aberrant stromule biogenesis in the leaf epidermis associated with giant and pleomorphic amoeboid chloroplasts, typically having one or more constrictions as well as one or more extremely long stromules (PubMed:28984364). Reduced number of enlarged etioplasts in cotyledons associated with the formation of multiple FtsZ-rings (PubMed:23936263).

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