CapA family protein similar to Bacillus anthracis capsule biosynthesis protein CapA, which is essential for the synthesis of its polyglutamate capsule and may form a polyglutamyl synthetase complex together with proteins CapB and CapC; belongs to the metallophosphoesterase (MPP) superfamily
Bacterial capsule synthesis protein PGA_cap; This protein is a putative poly-gamma-glutamate ...
34-239
8.99e-52
Bacterial capsule synthesis protein PGA_cap; This protein is a putative poly-gamma-glutamate capsule biosynthesis protein found in bacteria. Poly-gamma-glutamate is a natural polymer that may be involved in virulence and may help bacteria survive in high salt concentrations. It is a surface-associated protein.
Pssm-ID: 214858 [Multi-domain] Cd Length: 239 Bit Score: 172.39 E-value: 8.99e-52
Bacterial capsule synthesis protein PGA_cap; This protein is a putative poly-gamma-glutamate ...
34-239
1.98e-50
Bacterial capsule synthesis protein PGA_cap; This protein is a putative poly-gamma-glutamate capsule biosynthesis protein found in bacteria. Poly-gamma-glutamate is a natural polymer that may be involved in virulence and may help bacteria survive in high salt concentrations. It is a surface-associated protein.
Pssm-ID: 430701 [Multi-domain] Cd Length: 246 Bit Score: 169.33 E-value: 1.98e-50
CapA and related proteins, metallophosphatase domain; CapA is one of three membrane-associated ...
8-237
3.75e-47
CapA and related proteins, metallophosphatase domain; CapA is one of three membrane-associated enzymes in Bacillus anthracis that is required for synthesis of gamma-polyglutamic acid (PGA), a major component of the bacterial capsule. The YwtB and PgsA proteins of Bacillus subtilis are closely related to CapA and are also included in this alignment model. CapA belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.
Pssm-ID: 277327 [Multi-domain] Cd Length: 239 Bit Score: 160.53 E-value: 3.75e-47
Bacterial capsule synthesis protein PGA_cap; This protein is a putative poly-gamma-glutamate ...
34-239
8.99e-52
Bacterial capsule synthesis protein PGA_cap; This protein is a putative poly-gamma-glutamate capsule biosynthesis protein found in bacteria. Poly-gamma-glutamate is a natural polymer that may be involved in virulence and may help bacteria survive in high salt concentrations. It is a surface-associated protein.
Pssm-ID: 214858 [Multi-domain] Cd Length: 239 Bit Score: 172.39 E-value: 8.99e-52
Bacterial capsule synthesis protein PGA_cap; This protein is a putative poly-gamma-glutamate ...
34-239
1.98e-50
Bacterial capsule synthesis protein PGA_cap; This protein is a putative poly-gamma-glutamate capsule biosynthesis protein found in bacteria. Poly-gamma-glutamate is a natural polymer that may be involved in virulence and may help bacteria survive in high salt concentrations. It is a surface-associated protein.
Pssm-ID: 430701 [Multi-domain] Cd Length: 246 Bit Score: 169.33 E-value: 1.98e-50
CapA and related proteins, metallophosphatase domain; CapA is one of three membrane-associated ...
8-237
3.75e-47
CapA and related proteins, metallophosphatase domain; CapA is one of three membrane-associated enzymes in Bacillus anthracis that is required for synthesis of gamma-polyglutamic acid (PGA), a major component of the bacterial capsule. The YwtB and PgsA proteins of Bacillus subtilis are closely related to CapA and are also included in this alignment model. CapA belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.
Pssm-ID: 277327 [Multi-domain] Cd Length: 239 Bit Score: 160.53 E-value: 3.75e-47
Escherichia coli UshA-like family, N-terminal metallophosphatase domain; This family includes ...
87-185
2.05e-03
Escherichia coli UshA-like family, N-terminal metallophosphatase domain; This family includes the bacterial enzyme UshA, and related enzymes including SoxB, CpdB, YhcR, and CD73. All members have a similar domain architecture which includes an N-terminal metallophosphatase domain and a C-terminal nucleotidase domain. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.
Pssm-ID: 277323 [Multi-domain] Cd Length: 255 Bit Score: 39.60 E-value: 2.05e-03
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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