alginate O-acetyltransferase similar to Pseudomonas aeruginosa AlgJ which together with AlgI and AlgF may form an inner membrane complex that interacts with the alginate polymerisation/secretion multiprotein complex to mediate O-acetylation of nascent alginate
putative alginate O-acetyltranferases AlgJ, AlgV, and similar proteins; The alginate ...
47-374
3.23e-173
putative alginate O-acetyltranferases AlgJ, AlgV, and similar proteins; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. Its N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. Members of this family have been annotated as AlgJ or AlgV, and they closely resemble AlgX in sequence and function, although they lack the C-terminal carbohydrate binding domain of AlgX.
:
Pssm-ID: 270208 Cd Length: 321 Bit Score: 485.65 E-value: 3.23e-173
putative alginate O-acetyltranferases AlgJ, AlgV, and similar proteins; The alginate ...
47-374
3.23e-173
putative alginate O-acetyltranferases AlgJ, AlgV, and similar proteins; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. Its N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. Members of this family have been annotated as AlgJ or AlgV, and they closely resemble AlgX in sequence and function, although they lack the C-terminal carbohydrate binding domain of AlgX.
Pssm-ID: 270208 Cd Length: 321 Bit Score: 485.65 E-value: 3.23e-173
SGNH hydrolase-like domain, acetyltransferase AlgX; ALGX is a family found in bacteria. The ...
85-355
6.51e-111
SGNH hydrolase-like domain, acetyltransferase AlgX; ALGX is a family found in bacteria. The domain demonstrates catalytic activity similar to that of the SGNH hydrolase-like domain, with the typical Ser-His-Asp triad found in this enzyme. Alginate is an exopolysaccharide that contributes to biofilm formation. ALGX is secreted into the biofilm and is responsible for the acetylation of biofilm polymers that help protect them from host destruction.
Pssm-ID: 435599 Cd Length: 267 Bit Score: 325.45 E-value: 6.51e-111
putative alginate O-acetyltranferases AlgJ, AlgV, and similar proteins; The alginate ...
47-374
3.23e-173
putative alginate O-acetyltranferases AlgJ, AlgV, and similar proteins; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. Its N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. Members of this family have been annotated as AlgJ or AlgV, and they closely resemble AlgX in sequence and function, although they lack the C-terminal carbohydrate binding domain of AlgX.
Pssm-ID: 270208 Cd Length: 321 Bit Score: 485.65 E-value: 3.23e-173
SGNH hydrolase-like domain, acetyltransferase AlgX; ALGX is a family found in bacteria. The ...
85-355
6.51e-111
SGNH hydrolase-like domain, acetyltransferase AlgX; ALGX is a family found in bacteria. The domain demonstrates catalytic activity similar to that of the SGNH hydrolase-like domain, with the typical Ser-His-Asp triad found in this enzyme. Alginate is an exopolysaccharide that contributes to biofilm formation. ALGX is secreted into the biofilm and is responsible for the acetylation of biofilm polymers that help protect them from host destruction.
Pssm-ID: 435599 Cd Length: 267 Bit Score: 325.45 E-value: 6.51e-111
N-terminal catalytic domain of putative alginate O-acetyltranferase and similar proteins; The ...
49-359
1.39e-60
N-terminal catalytic domain of putative alginate O-acetyltranferase and similar proteins; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. Its N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. This wider family includes AlgX, AlgJ, AlgV, and a number of uncharacterized families, some of which may have been mis-annotated in sequence databases.
Pssm-ID: 270205 [Multi-domain] Cd Length: 316 Bit Score: 198.45 E-value: 1.39e-60
Uncharacterized proteins similar to putative alginate O-acetyltranferase; The alginate ...
68-360
3.58e-56
Uncharacterized proteins similar to putative alginate O-acetyltranferase; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such those as by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. Its N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. Members of this uncharacterized family similar to AlgX_N have been annotated as cell division proteins FtsQ, although they share little or no similarity with experimentally characterized members of the FtsQ family.
Pssm-ID: 270210 Cd Length: 298 Bit Score: 186.37 E-value: 3.58e-56
N-terminal catalytic domain of the putative alginate O-acetyltranferase AlgX; The alginate ...
75-366
4.02e-51
N-terminal catalytic domain of the putative alginate O-acetyltranferase AlgX; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. This N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. AlgX contains a C-terminal carbohydrate binding domain that belongs to the wider family of CBM6-CBM35-CBM36_like domains.
Pssm-ID: 270207 Cd Length: 310 Bit Score: 173.65 E-value: 4.02e-51
Uncharacterized proteins similar to putative alginate O-acetyltransferase; The alginate ...
56-245
1.39e-23
Uncharacterized proteins similar to putative alginate O-acetyltransferase; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. Its N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. Members of this uncharacterized protein family resemble AlgX_N.
Pssm-ID: 270206 [Multi-domain] Cd Length: 315 Bit Score: 99.74 E-value: 1.39e-23
Uncharacterized proteins similar to putative alginate O-acetyltranferase; The alginate ...
85-355
8.39e-23
Uncharacterized proteins similar to putative alginate O-acetyltranferase; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. Its N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. Some members of this uncharacterized family, which resembles AlgX_N, have been annotated as twin-arginine translocation signal, although they share little or no similarity with experimentally characterized proteins that bear the same name.
Pssm-ID: 270209 Cd Length: 313 Bit Score: 97.48 E-value: 8.39e-23
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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