ExbD/TolR family protein similar to biopolymer transporter ExbD, part of a complex that energizes specific high-affinity receptors involved in regulating iron uptake
TolR protein; The model describes the inner membrane protein TolR, part of the TolR/TolQ ...
12-133
1.09e-32
TolR protein; The model describes the inner membrane protein TolR, part of the TolR/TolQ complex that transduces energy from the proton-motive force, through TolA, to an outer membrane complex made up of TolB and Pal (peptidoglycan-associated lipoprotein). The complex is required to maintain outer membrane integrity, and defects may cause a defect in the import of some organic compounds in addition to the resulting morphologic. While several gene pairs homologous to talR and tolQ may be found in a single genome, but the scope of this model is set to favor finding only bone fide TolR, supported by operon structure as well as by score. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274306 Cd Length: 129 Bit Score: 111.93 E-value: 1.09e-32
Biopolymer transport protein ExbD/TolR; This group of proteins are membrane bound transport ...
9-135
2.06e-32
Biopolymer transport protein ExbD/TolR; This group of proteins are membrane bound transport proteins essential for ferric ion uptake in bacteria. The Pfam family consists of ExbD, and TolR which are involved in TonB-dependent transport of various receptor bound substrates including colicins.
Pssm-ID: 426791 Cd Length: 128 Bit Score: 111.21 E-value: 2.06e-32
TolR protein; The model describes the inner membrane protein TolR, part of the TolR/TolQ ...
12-133
1.09e-32
TolR protein; The model describes the inner membrane protein TolR, part of the TolR/TolQ complex that transduces energy from the proton-motive force, through TolA, to an outer membrane complex made up of TolB and Pal (peptidoglycan-associated lipoprotein). The complex is required to maintain outer membrane integrity, and defects may cause a defect in the import of some organic compounds in addition to the resulting morphologic. While several gene pairs homologous to talR and tolQ may be found in a single genome, but the scope of this model is set to favor finding only bone fide TolR, supported by operon structure as well as by score. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274306 Cd Length: 129 Bit Score: 111.93 E-value: 1.09e-32
Biopolymer transport protein ExbD/TolR; This group of proteins are membrane bound transport ...
9-135
2.06e-32
Biopolymer transport protein ExbD/TolR; This group of proteins are membrane bound transport proteins essential for ferric ion uptake in bacteria. The Pfam family consists of ExbD, and TolR which are involved in TonB-dependent transport of various receptor bound substrates including colicins.
Pssm-ID: 426791 Cd Length: 128 Bit Score: 111.21 E-value: 2.06e-32
TonB system transport protein ExbD, group 1; Members of this family are Gram-negative ...
13-124
6.28e-12
TonB system transport protein ExbD, group 1; Members of this family are Gram-negative bacterial inner membrane proteins, generally designated ExbD, related to the TolR family modeled by TIGRFAMs TIGR02801. Members always are encoded next to a protein designated ExbB (TIGR02797), related to the TolQ family modeled by TIGRFAMs TIGR02796. ExbD and ExbB together form a proton channel through which they can harness the proton-motive force to energize TonB, which in turn energizes TonB-dependent receptors in the outer membrane. TonB-dependent receptors with known specificity tend to import siderophores or vitamin B12. A TonB system and Tol-Pal system often will co-exist in a single bacterial genome.
Pssm-ID: 131850 Cd Length: 122 Bit Score: 58.69 E-value: 6.28e-12
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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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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specific hits meet or exceed a domain-specific e-value threshold
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