PTS beta-glucoside transporter subunit IIBCA catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane
PTS system, sucrose-specific IIBC component; This model represents the fused enzyme II B and C ...
2-457
0e+00
PTS system, sucrose-specific IIBC component; This model represents the fused enzyme II B and C components of the sucrose-specific PTS sugar transporter system. Sucrose is converted to sucrose-6-phosphate in the process of translocation into the cell. Some of these transporters lack their own IIA domains and instead use the glucose IIA protein (IIAglc or Crr). The exceptions to this rule are Staphylococci, Streptococci, Lactococci, Lactobacilli, etc. which contain their own A domain as a C-terminal fusion. This family is closely related to the trehalose transporting PTS IIBC enzymes and the B and C domains of each are described by subfamily-domain level TIGRFAMs models (TIGR00826 and TIGR00852, respectively).
:
Pssm-ID: 131051 Cd Length: 461 Bit Score: 603.91 E-value: 0e+00
PTS system, sucrose-specific IIBC component; This model represents the fused enzyme II B and C ...
2-457
0e+00
PTS system, sucrose-specific IIBC component; This model represents the fused enzyme II B and C components of the sucrose-specific PTS sugar transporter system. Sucrose is converted to sucrose-6-phosphate in the process of translocation into the cell. Some of these transporters lack their own IIA domains and instead use the glucose IIA protein (IIAglc or Crr). The exceptions to this rule are Staphylococci, Streptococci, Lactococci, Lactobacilli, etc. which contain their own A domain as a C-terminal fusion. This family is closely related to the trehalose transporting PTS IIBC enzymes and the B and C domains of each are described by subfamily-domain level TIGRFAMs models (TIGR00826 and TIGR00852, respectively).
Pssm-ID: 131051 Cd Length: 461 Bit Score: 603.91 E-value: 0e+00
PTS_IIA, PTS system, glucose/sucrose specific IIA subunit. The bacterial phosphoenolpyruvate: ...
499-622
1.16e-58
PTS_IIA, PTS system, glucose/sucrose specific IIA subunit. The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is a multi-protein system involved in the regulation of a variety of metabolic and transcriptional processes. This family is one of four structurally and functionally distinct group IIA PTS system cytoplasmic enzymes, necessary for the uptake of carbohydrates across the cytoplasmic membrane and their phosphorylation.
Pssm-ID: 238128 [Multi-domain] Cd Length: 124 Bit Score: 192.89 E-value: 1.16e-58
PTS system, glucose subfamily, IIA component; These are part of the The PTS Glucose-Glucoside ...
499-619
1.62e-55
PTS system, glucose subfamily, IIA component; These are part of the The PTS Glucose-Glucoside (Glc) SuperFamily. The Glc family includes permeases specific for glucose, N-acetylglucosamine and a large variety of a- and b-glucosides. However, not all b-glucoside PTS permeases are in this class, as the cellobiose (Cel) b-glucoside PTS permease is in the Lac family (TC #4.A.3). The IIA, IIB and IIC domains of all of the permeases listed below are demonstrably homologous. These permeases show limited sequence similarity with members of the Fru family (TC #4.A.2). Several of the PTS permeases in the Glc family lack their own IIA domains and instead use the glucose IIA protein (IIAglc or Crr). Most of these permeases have the B and C domains linked together in a single polypeptide chain, and a cysteyl residue in the IIB domain is phosphorylated by direct phosphoryl transfer from IIAglc(his~P). Those permeases which lack a IIA domain include the maltose (Mal), arbutin-salicin-cellobiose (ASC), trehalose (Tre), putative glucoside (Glv) and sucrose (Scr) permeases of E. coli . Most, but not all Scr permeases of other bacteria also lack a IIA domain. The three-dimensional structures of the IIA and IIB domains of the E. coli glucose permease have been elucidated. IIAglchas a complex b-sandwich structure while IIBglc is a split ab-sandwich with a topology unrelated to the split ab-sandwich structure of HPr. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS]
Pssm-ID: 273289 [Multi-domain] Cd Length: 121 Bit Score: 184.37 E-value: 1.62e-55
Phosphotransferase system, EIIC; The bacterial phosphoenolpyruvate: sugar phosphotransferase ...
111-397
1.25e-50
Phosphotransferase system, EIIC; The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is a multi-protein system involved in the regulation of a variety of metabolic and transcriptional processes. The sugar-specific permease of the PTS consists of three domains (IIA, IIB and IIC). The IIC domain catalyzes the transfer of a phosphoryl group from IIB to the sugar substrate.
Pssm-ID: 367061 Cd Length: 315 Bit Score: 177.92 E-value: 1.25e-50
PTS_IIB, PTS system, glucose/sucrose specific IIB subunit. The bacterial phosphoenolpyruvate: ...
4-81
2.94e-25
PTS_IIB, PTS system, glucose/sucrose specific IIB subunit. The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is a multi-protein system involved in the regulation of a variety of metabolic and transcriptional processes. This family is one of four structurally and functionally distinct group IIB PTS system cytoplasmic enzymes, necessary for the uptake of carbohydrates across the cytoplasmic membrane and their phosphorylation
Pssm-ID: 238130 [Multi-domain] Cd Length: 78 Bit Score: 99.53 E-value: 2.94e-25
PTS system, sucrose-specific IIBC component; This model represents the fused enzyme II B and C ...
2-457
0e+00
PTS system, sucrose-specific IIBC component; This model represents the fused enzyme II B and C components of the sucrose-specific PTS sugar transporter system. Sucrose is converted to sucrose-6-phosphate in the process of translocation into the cell. Some of these transporters lack their own IIA domains and instead use the glucose IIA protein (IIAglc or Crr). The exceptions to this rule are Staphylococci, Streptococci, Lactococci, Lactobacilli, etc. which contain their own A domain as a C-terminal fusion. This family is closely related to the trehalose transporting PTS IIBC enzymes and the B and C domains of each are described by subfamily-domain level TIGRFAMs models (TIGR00826 and TIGR00852, respectively).
Pssm-ID: 131051 Cd Length: 461 Bit Score: 603.91 E-value: 0e+00
PTS system, beta-glucoside-specific IIABC component; This model represents a family of PTS ...
3-643
6.78e-172
PTS system, beta-glucoside-specific IIABC component; This model represents a family of PTS enzyme II proteins in which all three domains are found in the same polypeptide chain and which appear to have a broad specificity for beta-glucosides including salicin (beta-D-glucose-1-salicylate) and arbutin (Hydroquinone-O-beta-D-glucopyranoside). These are distinct from the closely related sucrose-specific and trehalose-specific PTS transporters.
Pssm-ID: 273919 [Multi-domain] Cd Length: 610 Bit Score: 503.42 E-value: 6.78e-172
PTS system, trehalose-specific IIBC component; This model represents the fused enzyme II B and ...
4-459
1.08e-140
PTS system, trehalose-specific IIBC component; This model represents the fused enzyme II B and C components of the trehalose-specific PTS sugar transporter system. Trehalose is converted to trehalose-6-phosphate in the process of translocation into the cell. These transporters lack their own IIA domains and instead use the glucose IIA protein (IIAglc or Crr). The exceptions to this rule are Staphylococci and Streptococci which contain their own A domain as a C-terminal fusion. This family is closely related to the sucrose transporting PTS IIBC enzymes and the B and C domains of each are described by subfamily-domain level TIGRFAMs models (TIGR00826 and TIGR00852, respectively). In E. coli, B. subtilis and P. fluorescens the presence of this gene is associated with the presence of trehalase which degrades T6P to glucose and glucose-6-P. Trehalose may also be transported (in Salmonella) via the mannose PTS or galactose permease systems, or (in Sinorhizobium, Thermococcus and Sulfolobus, for instance) by ABC transporters.
Pssm-ID: 273916 Cd Length: 462 Bit Score: 417.98 E-value: 1.08e-140
PTS_IIA, PTS system, glucose/sucrose specific IIA subunit. The bacterial phosphoenolpyruvate: ...
499-622
1.16e-58
PTS_IIA, PTS system, glucose/sucrose specific IIA subunit. The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is a multi-protein system involved in the regulation of a variety of metabolic and transcriptional processes. This family is one of four structurally and functionally distinct group IIA PTS system cytoplasmic enzymes, necessary for the uptake of carbohydrates across the cytoplasmic membrane and their phosphorylation.
Pssm-ID: 238128 [Multi-domain] Cd Length: 124 Bit Score: 192.89 E-value: 1.16e-58
PTS system, glucose subfamily, IIA component; These are part of the The PTS Glucose-Glucoside ...
499-619
1.62e-55
PTS system, glucose subfamily, IIA component; These are part of the The PTS Glucose-Glucoside (Glc) SuperFamily. The Glc family includes permeases specific for glucose, N-acetylglucosamine and a large variety of a- and b-glucosides. However, not all b-glucoside PTS permeases are in this class, as the cellobiose (Cel) b-glucoside PTS permease is in the Lac family (TC #4.A.3). The IIA, IIB and IIC domains of all of the permeases listed below are demonstrably homologous. These permeases show limited sequence similarity with members of the Fru family (TC #4.A.2). Several of the PTS permeases in the Glc family lack their own IIA domains and instead use the glucose IIA protein (IIAglc or Crr). Most of these permeases have the B and C domains linked together in a single polypeptide chain, and a cysteyl residue in the IIB domain is phosphorylated by direct phosphoryl transfer from IIAglc(his~P). Those permeases which lack a IIA domain include the maltose (Mal), arbutin-salicin-cellobiose (ASC), trehalose (Tre), putative glucoside (Glv) and sucrose (Scr) permeases of E. coli . Most, but not all Scr permeases of other bacteria also lack a IIA domain. The three-dimensional structures of the IIA and IIB domains of the E. coli glucose permease have been elucidated. IIAglchas a complex b-sandwich structure while IIBglc is a split ab-sandwich with a topology unrelated to the split ab-sandwich structure of HPr. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS]
Pssm-ID: 273289 [Multi-domain] Cd Length: 121 Bit Score: 184.37 E-value: 1.62e-55
Phosphotransferase system, EIIC; The bacterial phosphoenolpyruvate: sugar phosphotransferase ...
111-397
1.25e-50
Phosphotransferase system, EIIC; The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is a multi-protein system involved in the regulation of a variety of metabolic and transcriptional processes. The sugar-specific permease of the PTS consists of three domains (IIA, IIB and IIC). The IIC domain catalyzes the transfer of a phosphoryl group from IIB to the sugar substrate.
Pssm-ID: 367061 Cd Length: 315 Bit Score: 177.92 E-value: 1.25e-50
PTS_IIB, PTS system, glucose/sucrose specific IIB subunit. The bacterial phosphoenolpyruvate: ...
4-81
2.94e-25
PTS_IIB, PTS system, glucose/sucrose specific IIB subunit. The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is a multi-protein system involved in the regulation of a variety of metabolic and transcriptional processes. This family is one of four structurally and functionally distinct group IIB PTS system cytoplasmic enzymes, necessary for the uptake of carbohydrates across the cytoplasmic membrane and their phosphorylation
Pssm-ID: 238130 [Multi-domain] Cd Length: 78 Bit Score: 99.53 E-value: 2.94e-25
PTS system, glucose-like IIB component; The PTS Glucose-Glucoside (Glc) Family (TC 4.A.1) ...
27-112
2.80e-13
PTS system, glucose-like IIB component; The PTS Glucose-Glucoside (Glc) Family (TC 4.A.1) Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains. The Glc family includes permeases specific for glucose, N-acetylglucosamine and a large variety of a- and b-glucosides. However, not all b-glucoside PTS permeases are in this class, as the cellobiose (Cel) b-glucoside PTS permease is in the Lac family (TC #4.A.3). These permeases show limited sequence similarity with members of the Fru family (TC #4.A.2). Several of the E. coli PTS permeases in the Glc family lack their own IIA domains and instead use the glucose IIA protein (IIAglc or Crr). Most of these permeases have the B and C domains linked together in a single polypeptide chain, and a cysteyl residue in the IIB domain is phosphorylated by direct phosphoryl transfer from IIAglc(his~P). Those permeases which lack a IIA domain include the maltose (Mal), arbutin-salicin-cellobiose (ASC), trehalose (Tre), putative glucoside (Glv) and sucrose (Scr) permeases of E. coli . Most, but not all Scr permeases of other bacteria also lack a IIA domain. This model is specific for the IIB domain of the Glc family PTS transporters. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS]
Pssm-ID: 273288 [Multi-domain] Cd Length: 88 Bit Score: 65.84 E-value: 2.80e-13
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
531-599
2.47e-03
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.
Pssm-ID: 410984 [Multi-domain] Cd Length: 85 Bit Score: 37.19 E-value: 2.47e-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.
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