permease-like cell division protein FtsX; The FtsEX complex resembles an ABC transporter, ...
2-295
9.16e-164
permease-like cell division protein FtsX; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages.
The actual alignment was detected with superfamily member NF038347:
Pssm-ID: 468488 [Multi-domain] Cd Length: 296 Bit Score: 456.51 E-value: 9.16e-164
permease-like cell division protein FtsX; The FtsEX complex resembles an ABC transporter, ...
2-295
9.16e-164
permease-like cell division protein FtsX; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages.
Pssm-ID: 468488 [Multi-domain] Cd Length: 296 Bit Score: 456.51 E-value: 9.16e-164
FtsX extracellular domain; This is the extracellular domain (ECD) found in FtsX enzyme, a ...
58-151
9.10e-28
FtsX extracellular domain; This is the extracellular domain (ECD) found in FtsX enzyme, a homolog of the transmembrane PG-hydrolase regulator. The FtsX extracellular domain binds the PG peptidase Rv2190c/RipC N-terminal segment, causing a conformational change that activates the enzyme ileading to PG hydrolysis in Mycobacterium tuberculosis. Structural analysis of FtsX ECD reveals fold containing two lobes connected by a flexible hinge. Mutations in the hydrophobic cleft between the lobes showed reduction in RipC binding in vitro and inhibition of FtsX function in Mycobacterium smegmatis.
Pssm-ID: 465634 [Multi-domain] Cd Length: 94 Bit Score: 102.96 E-value: 9.10e-28
putative protein insertion permease FtsX; FtsX is an integral membrane protein encoded in the ...
8-284
7.38e-25
putative protein insertion permease FtsX; FtsX is an integral membrane protein encoded in the same operon as signal recognition particle docking protein FtsY and FtsE. It belongs to a family of predicted permeases and may play a role in the insertion of proteins required for potassium transport, cell division, and other activities. FtsE is a hydrophilic nucleotide-binding protein that associates with the inner membrane by means of association with FtsX. [Cellular processes, Cell division, Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 129531 [Multi-domain] Cd Length: 309 Bit Score: 101.47 E-value: 7.38e-25
putative protein insertion permease FtsX; FtsX is an integral membrane protein encoded in the ...
9-282
1.95e-22
putative protein insertion permease FtsX; FtsX is an integral membrane protein encoded in the same operon as signal recognition particle docking protein FtsY and FtsE. It belongs to a family of predicted permeases and may play a role in the insertion of proteins required for potassium transport, cell division, and other activities. FtsE is a hydrophilic nucleotide-binding protein that associates with the inner membrane by means of association with FtsX. [Cellular processes, Cell division, Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 182910 [Multi-domain] Cd Length: 309 Bit Score: 94.66 E-value: 1.95e-22
permease-like cell division protein FtsX; The FtsEX complex resembles an ABC transporter, ...
2-295
9.16e-164
permease-like cell division protein FtsX; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages.
Pssm-ID: 468488 [Multi-domain] Cd Length: 296 Bit Score: 456.51 E-value: 9.16e-164
FtsX extracellular domain; This is the extracellular domain (ECD) found in FtsX enzyme, a ...
58-151
9.10e-28
FtsX extracellular domain; This is the extracellular domain (ECD) found in FtsX enzyme, a homolog of the transmembrane PG-hydrolase regulator. The FtsX extracellular domain binds the PG peptidase Rv2190c/RipC N-terminal segment, causing a conformational change that activates the enzyme ileading to PG hydrolysis in Mycobacterium tuberculosis. Structural analysis of FtsX ECD reveals fold containing two lobes connected by a flexible hinge. Mutations in the hydrophobic cleft between the lobes showed reduction in RipC binding in vitro and inhibition of FtsX function in Mycobacterium smegmatis.
Pssm-ID: 465634 [Multi-domain] Cd Length: 94 Bit Score: 102.96 E-value: 9.10e-28
putative protein insertion permease FtsX; FtsX is an integral membrane protein encoded in the ...
8-284
7.38e-25
putative protein insertion permease FtsX; FtsX is an integral membrane protein encoded in the same operon as signal recognition particle docking protein FtsY and FtsE. It belongs to a family of predicted permeases and may play a role in the insertion of proteins required for potassium transport, cell division, and other activities. FtsE is a hydrophilic nucleotide-binding protein that associates with the inner membrane by means of association with FtsX. [Cellular processes, Cell division, Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 129531 [Multi-domain] Cd Length: 309 Bit Score: 101.47 E-value: 7.38e-25
putative protein insertion permease FtsX; FtsX is an integral membrane protein encoded in the ...
9-282
1.95e-22
putative protein insertion permease FtsX; FtsX is an integral membrane protein encoded in the same operon as signal recognition particle docking protein FtsY and FtsE. It belongs to a family of predicted permeases and may play a role in the insertion of proteins required for potassium transport, cell division, and other activities. FtsE is a hydrophilic nucleotide-binding protein that associates with the inner membrane by means of association with FtsX. [Cellular processes, Cell division, Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 182910 [Multi-domain] Cd Length: 309 Bit Score: 94.66 E-value: 1.95e-22
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease ...
172-296
1.75e-10
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442361 [Multi-domain] Cd Length: 830 Bit Score: 61.36 E-value: 1.75e-10
FtsX-like permease family; This is a family of predicted permeases and hypothetical ...
173-292
4.09e-10
FtsX-like permease family; This is a family of predicted permeases and hypothetical transmembrane proteins. Swiss:P57382 has been shown to transport lipids targeted to the outer membrane across the inner membrane. Both Swiss:P57382 and Swiss:O54500 have been shown to require ATP. This region contains three transmembrane helices.
Pssm-ID: 460652 [Multi-domain] Cd Length: 120 Bit Score: 56.49 E-value: 4.09e-10
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease ...
166-283
3.45e-08
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442361 [Multi-domain] Cd Length: 830 Bit Score: 54.42 E-value: 3.45e-08
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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