oligogalacturonate lyase family protein similar to Dickeya dadantii oligogalacturonate lyase that catalyzes the conversion of saturated and unsaturated digalacturonate into monogalacturonate using a beta-elimination mechanism
Oligogalacturonate lyase; This is a family of oligogalacturonate lyases, referred to more ...
1-386
0e+00
Oligogalacturonate lyase; This is a family of oligogalacturonate lyases, referred to more generally as pectate lyase family 22. These proteins fold into 7-bladed beta-propellers.
:
Pssm-ID: 434052 [Multi-domain] Cd Length: 386 Bit Score: 838.52 E-value: 0e+00
Oligogalacturonate lyase; This is a family of oligogalacturonate lyases, referred to more ...
1-386
0e+00
Oligogalacturonate lyase; This is a family of oligogalacturonate lyases, referred to more generally as pectate lyase family 22. These proteins fold into 7-bladed beta-propellers.
Pssm-ID: 434052 [Multi-domain] Cd Length: 386 Bit Score: 838.52 E-value: 0e+00
tol-pal system beta propeller repeat protein TolB; Members of this protein family are the TolB ...
245-378
1.10e-05
tol-pal system beta propeller repeat protein TolB; Members of this protein family are the TolB periplasmic protein of Gram-negative bacteria. TolB is part of the Tol-Pal (peptidoglycan-associated lipoprotein) multiprotein complex, comprising five envelope proteins, TolQ, TolR, TolA, TolB and Pal, which form two complexes. The TolQ, TolR and TolA inner-membrane proteins interact via their transmembrane domains. The {beta}-propeller domain of the periplasmic protein TolB is responsible for its interaction with Pal. TolB also interacts with the outer-membrane peptidoglycan-associated proteins Lpp and OmpA. TolA undergoes a conformational change in response to changes in the proton-motive force, and interacts with Pal in an energy-dependent manner. The C-terminal periplasmic domain of TolA also interacts with the N-terminal domain of TolB. The Tol-PAL system is required for bacterial outer membrane integrity. E. coli TolB is involved in the tonB-independent uptake of group A colicins (colicins A, E1, E2, E3 and K), and is necessary for the colicins to reach their respective targets after initial binding to the bacteria. It is also involved in uptake of filamentous DNA. Study of its structure suggest that the TolB protein might be involved in the recycling of peptidoglycan or in its covalent linking with lipoproteins. The Tol-Pal system is also implicated in pathogenesis of E. coli, Haemophilus ducreyi , Salmonella enterica and Vibrio cholerae, but the mechanism(s) is unclear. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274305 [Multi-domain] Cd Length: 417 Bit Score: 47.27 E-value: 1.10e-05
Oligogalacturonate lyase; This is a family of oligogalacturonate lyases, referred to more ...
1-386
0e+00
Oligogalacturonate lyase; This is a family of oligogalacturonate lyases, referred to more generally as pectate lyase family 22. These proteins fold into 7-bladed beta-propellers.
Pssm-ID: 434052 [Multi-domain] Cd Length: 386 Bit Score: 838.52 E-value: 0e+00
tol-pal system beta propeller repeat protein TolB; Members of this protein family are the TolB ...
245-378
1.10e-05
tol-pal system beta propeller repeat protein TolB; Members of this protein family are the TolB periplasmic protein of Gram-negative bacteria. TolB is part of the Tol-Pal (peptidoglycan-associated lipoprotein) multiprotein complex, comprising five envelope proteins, TolQ, TolR, TolA, TolB and Pal, which form two complexes. The TolQ, TolR and TolA inner-membrane proteins interact via their transmembrane domains. The {beta}-propeller domain of the periplasmic protein TolB is responsible for its interaction with Pal. TolB also interacts with the outer-membrane peptidoglycan-associated proteins Lpp and OmpA. TolA undergoes a conformational change in response to changes in the proton-motive force, and interacts with Pal in an energy-dependent manner. The C-terminal periplasmic domain of TolA also interacts with the N-terminal domain of TolB. The Tol-PAL system is required for bacterial outer membrane integrity. E. coli TolB is involved in the tonB-independent uptake of group A colicins (colicins A, E1, E2, E3 and K), and is necessary for the colicins to reach their respective targets after initial binding to the bacteria. It is also involved in uptake of filamentous DNA. Study of its structure suggest that the TolB protein might be involved in the recycling of peptidoglycan or in its covalent linking with lipoproteins. The Tol-Pal system is also implicated in pathogenesis of E. coli, Haemophilus ducreyi , Salmonella enterica and Vibrio cholerae, but the mechanism(s) is unclear. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274305 [Multi-domain] Cd Length: 417 Bit Score: 47.27 E-value: 1.10e-05
WD40-like Beta Propeller Repeat; This family appears to be related to the pfam00400 repeat. ...
356-378
1.00e-03
WD40-like Beta Propeller Repeat; This family appears to be related to the pfam00400 repeat. This repeat corresponds to the RIVW repeat identified in cell surface proteins [Adindla et al. Comparative and Functional Genomics 2004; 5:2-16].
Pssm-ID: 429587 [Multi-domain] Cd Length: 37 Bit Score: 36.34 E-value: 1.00e-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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Functional characterization of the conserved domain architecture found on the query.
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