murein biosynthesis integral membrane protein MurJ (MviN) containing an intracellular pseudokinase domain, may function as the peptidoglycan lipid II flippase which is involved in translocation of lipid-anchored peptidoglycan precursors across the cytoplasmic membrane
Pseudokinase domain of the peptidoglycan biosynthetic protein MviN; The pseudokinase domain ...
694-924
9.67e-59
Pseudokinase domain of the peptidoglycan biosynthetic protein MviN; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This family is composed of the mycobacterial protein MviN and similar proteins. MviN is an integral membrane protein that is essential for growth and is required for cell wall integrity and peptidogylcan (PG) biosynthesis. It comprises of 14 predicted transmembrane (TM) helices at the N-terminus, followed by an intracellular pseudokinase domain linked through a single TM helix to a carbohydrate binding extracellular domain. Phosphorylation of the MviN pseudokinase domain by the PG-sensitive serine/threonine protein kinase PknB recruits a forkhead associated (FHA) domain protein FhaA, which modulates local PG synthesis at cell poles and the septum. The MviN pseudokinase forms a canonical receptor kinase dimer.
:
Pssm-ID: 270875 [Multi-domain] Cd Length: 236 Bit Score: 201.79 E-value: 9.67e-59
MurJ/MviN, a subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins; ...
110-543
1.02e-97
MurJ/MviN, a subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins; Escherichia coli MurJ (MviN) has been identified as essential for murein biosynthesis. It has been suggested that MurJ functions as the peptidoglycan lipid II flippase which is involved in translocation of lipid-anchored peptidoglycan precursors across the cytoplasmic membrane, though results obtained in Bacillus subtilis seem to indicate that its MurJ homologs are not essential for growth. Some MviN family members (e.g. in Mycobacterium tuberculosis) possess an extended C-terminal region that contains an intracellular pseudo-kinase domain and an extracellular domain resembling carbohydrate-binding proteins. Proteins from the MATE family are involved in exporting metabolites across the cell membrane and are often responsible for multidrug resistance (MDR).
Pssm-ID: 240528 [Multi-domain] Cd Length: 420 Bit Score: 316.32 E-value: 1.02e-97
Lipid II flippase MurJ; Peptidoglycan synthesis (PG) biosynthesis involves the formation of ...
127-592
4.62e-76
Lipid II flippase MurJ; Peptidoglycan synthesis (PG) biosynthesis involves the formation of peptidoglycan precursor lipid II (undecaprenyl-pyrophosphate-linked N-acetyl glucosamine-N-acetyl muramic acid-pentapeptide) on the cytosolic face of the cell membrane. Lipid II is then translocated across the membrane and its glycopeptide moiety becomes incorporated into the growing cell wall mesh. MviN, renamed as MurJ, is a lipid II flippase essential for cell wall peptidoglycan synthesis. MurJ belongs to the MVF (mouse virulence factor) family of MOP superfamily transporters, which also includes the MATE (multidrug and toxic compound extrusion) transporter and eukaryotic OLF (oligosaccharidyl-lipid flippase) families. In addition to the canonical MOP transporter core consisting of 12 transmembrane helices (TMs), MurJ has two additional C-terminal TMs (13 and 14) of unknown function. Structural analysis indicates that the N lobe (TMs 1-6) and C lobe (TMs 7-14) are arranged in an inward-facing N-shape conformation, rather than the outward-facing V-shape conformation observed in all existing MATE transporter structures. Furthermore, a hydrophobic groove is formed by two C-terminal transmembrane helices, which leads into a large central cavity that is mostly cationic. Mutagenesis studies, revealed a solvent-exposed cavity that is essential for function. Mutation of conserved residues (Ser17, Arg18, Arg24, Arg52, and Arg255) at the proximal site failed to complement MurJ function, consistent with the idea that these residues are important for recognizing the diphosphate and/or sugar moieties of lipid II. It has also been suggested that the chloride ion in the central cavity and a zinc ion at the beginning of TM 7 might be functionally important.
Pssm-ID: 397249 [Multi-domain] Cd Length: 451 Bit Score: 258.37 E-value: 4.62e-76
murein biosynthesis integral membrane protein MurJ; This model represents MurJ (previously ...
102-625
6.59e-61
murein biosynthesis integral membrane protein MurJ; This model represents MurJ (previously MviN), a family of integral membrane proteins predicted to have ten or more transmembrane regions. Members have been suggested to act as a lipid II flippase, translocated a precursor of murein. However, it appears FtsW has that activity. Flippase activity for MurJ has not been shown. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273763 [Multi-domain] Cd Length: 502 Bit Score: 217.19 E-value: 6.59e-61
Pseudokinase domain of the peptidoglycan biosynthetic protein MviN; The pseudokinase domain ...
694-924
9.67e-59
Pseudokinase domain of the peptidoglycan biosynthetic protein MviN; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This family is composed of the mycobacterial protein MviN and similar proteins. MviN is an integral membrane protein that is essential for growth and is required for cell wall integrity and peptidogylcan (PG) biosynthesis. It comprises of 14 predicted transmembrane (TM) helices at the N-terminus, followed by an intracellular pseudokinase domain linked through a single TM helix to a carbohydrate binding extracellular domain. Phosphorylation of the MviN pseudokinase domain by the PG-sensitive serine/threonine protein kinase PknB recruits a forkhead associated (FHA) domain protein FhaA, which modulates local PG synthesis at cell poles and the septum. The MviN pseudokinase forms a canonical receptor kinase dimer.
Pssm-ID: 270875 [Multi-domain] Cd Length: 236 Bit Score: 201.79 E-value: 9.67e-59
MurJ/MviN, a subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins; ...
110-543
1.02e-97
MurJ/MviN, a subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins; Escherichia coli MurJ (MviN) has been identified as essential for murein biosynthesis. It has been suggested that MurJ functions as the peptidoglycan lipid II flippase which is involved in translocation of lipid-anchored peptidoglycan precursors across the cytoplasmic membrane, though results obtained in Bacillus subtilis seem to indicate that its MurJ homologs are not essential for growth. Some MviN family members (e.g. in Mycobacterium tuberculosis) possess an extended C-terminal region that contains an intracellular pseudo-kinase domain and an extracellular domain resembling carbohydrate-binding proteins. Proteins from the MATE family are involved in exporting metabolites across the cell membrane and are often responsible for multidrug resistance (MDR).
Pssm-ID: 240528 [Multi-domain] Cd Length: 420 Bit Score: 316.32 E-value: 1.02e-97
Lipid II flippase MurJ; Peptidoglycan synthesis (PG) biosynthesis involves the formation of ...
127-592
4.62e-76
Lipid II flippase MurJ; Peptidoglycan synthesis (PG) biosynthesis involves the formation of peptidoglycan precursor lipid II (undecaprenyl-pyrophosphate-linked N-acetyl glucosamine-N-acetyl muramic acid-pentapeptide) on the cytosolic face of the cell membrane. Lipid II is then translocated across the membrane and its glycopeptide moiety becomes incorporated into the growing cell wall mesh. MviN, renamed as MurJ, is a lipid II flippase essential for cell wall peptidoglycan synthesis. MurJ belongs to the MVF (mouse virulence factor) family of MOP superfamily transporters, which also includes the MATE (multidrug and toxic compound extrusion) transporter and eukaryotic OLF (oligosaccharidyl-lipid flippase) families. In addition to the canonical MOP transporter core consisting of 12 transmembrane helices (TMs), MurJ has two additional C-terminal TMs (13 and 14) of unknown function. Structural analysis indicates that the N lobe (TMs 1-6) and C lobe (TMs 7-14) are arranged in an inward-facing N-shape conformation, rather than the outward-facing V-shape conformation observed in all existing MATE transporter structures. Furthermore, a hydrophobic groove is formed by two C-terminal transmembrane helices, which leads into a large central cavity that is mostly cationic. Mutagenesis studies, revealed a solvent-exposed cavity that is essential for function. Mutation of conserved residues (Ser17, Arg18, Arg24, Arg52, and Arg255) at the proximal site failed to complement MurJ function, consistent with the idea that these residues are important for recognizing the diphosphate and/or sugar moieties of lipid II. It has also been suggested that the chloride ion in the central cavity and a zinc ion at the beginning of TM 7 might be functionally important.
Pssm-ID: 397249 [Multi-domain] Cd Length: 451 Bit Score: 258.37 E-value: 4.62e-76
murein biosynthesis integral membrane protein MurJ; This model represents MurJ (previously ...
102-625
6.59e-61
murein biosynthesis integral membrane protein MurJ; This model represents MurJ (previously MviN), a family of integral membrane proteins predicted to have ten or more transmembrane regions. Members have been suggested to act as a lipid II flippase, translocated a precursor of murein. However, it appears FtsW has that activity. Flippase activity for MurJ has not been shown. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273763 [Multi-domain] Cd Length: 502 Bit Score: 217.19 E-value: 6.59e-61
Pseudokinase domain of the peptidoglycan biosynthetic protein MviN; The pseudokinase domain ...
694-924
9.67e-59
Pseudokinase domain of the peptidoglycan biosynthetic protein MviN; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This family is composed of the mycobacterial protein MviN and similar proteins. MviN is an integral membrane protein that is essential for growth and is required for cell wall integrity and peptidogylcan (PG) biosynthesis. It comprises of 14 predicted transmembrane (TM) helices at the N-terminus, followed by an intracellular pseudokinase domain linked through a single TM helix to a carbohydrate binding extracellular domain. Phosphorylation of the MviN pseudokinase domain by the PG-sensitive serine/threonine protein kinase PknB recruits a forkhead associated (FHA) domain protein FhaA, which modulates local PG synthesis at cell poles and the septum. The MviN pseudokinase forms a canonical receptor kinase dimer.
Pssm-ID: 270875 [Multi-domain] Cd Length: 236 Bit Score: 201.79 E-value: 9.67e-59
Uncharacterized subfamily of the multidrug and toxic compound extrusion (MATE) proteins; This ...
104-431
1.19e-07
Uncharacterized subfamily of the multidrug and toxic compound extrusion (MATE) proteins; This family might function as a translocase for lipopolysaccharides, such as O-antigen. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. A number of family members are involved in the synthesis of peptidoglycan components in bacteria.
Pssm-ID: 240530 [Multi-domain] Cd Length: 409 Bit Score: 55.24 E-value: 1.19e-07
Stage V sporulation protein B, also known as Stage III sporulation protein F, and related ...
109-474
1.84e-07
Stage V sporulation protein B, also known as Stage III sporulation protein F, and related proteins; The integral membrane protein SpoVB has been implicated in the biosynthesis of the peptidoglycan component of the spore cortex in Bacillus subtilis. This model represents a subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins. Proteins from the MATE family are involved in exporting metabolites across the cell membrane and are often responsible for multidrug resistance (MDR).
Pssm-ID: 240529 [Multi-domain] Cd Length: 434 Bit Score: 54.78 E-value: 1.84e-07
Multidrug and toxic compound extrusion family and similar proteins; The integral membrane ...
107-492
3.50e-05
Multidrug and toxic compound extrusion family and similar proteins; The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. MATE has also been identified as a large multigene family in plants, where the proteins are linked to disease resistance. A number of family members are involved in the synthesis of peptidoglycan components in bacteria.
Pssm-ID: 240527 [Multi-domain] Cd Length: 420 Bit Score: 47.70 E-value: 3.50e-05
Uncharacterized subfamily of the multidrug and toxic compound extrusion (MATE) proteins; This ...
102-438
7.11e-04
Uncharacterized subfamily of the multidrug and toxic compound extrusion (MATE) proteins; This family might function as a translocase for lipopolysaccharides and participate in the biosynthesis of cell wall components such as teichuronic acid. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. A number of family members are involved in the synthesis of peptidoglycan components in bacteria.
Pssm-ID: 240532 [Multi-domain] Cd Length: 406 Bit Score: 43.24 E-value: 7.11e-04
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.
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