Putative threonine/serine exporter; ThrE is a family of bacterial and Archaeal proteins that ...
11-256
1.20e-59
Putative threonine/serine exporter; ThrE is a family of bacterial and Archaeal proteins that catalyze the export of L-threonine from the cell. UniProtKB:Q79VD1 has been characterized as being necessary for this export. The domain exhibits 10 putative TMs and catalyzes the proton-motive-force-dependent efflux of threonine and serine.
Pssm-ID: 461997 Cd Length: 241 Bit Score: 194.28 E-value: 1.20e-59
Putative threonine/serine exporter; ThrE is a family of bacterial and Archaeal proteins that ...
11-256
1.20e-59
Putative threonine/serine exporter; ThrE is a family of bacterial and Archaeal proteins that catalyze the export of L-threonine from the cell. UniProtKB:Q79VD1 has been characterized as being necessary for this export. The domain exhibits 10 putative TMs and catalyzes the proton-motive-force-dependent efflux of threonine and serine.
Pssm-ID: 461997 Cd Length: 241 Bit Score: 194.28 E-value: 1.20e-59
Threonine/Serine exporter, ThrE; ThrE_2 is a family of membrane proteins involved in the ...
280-403
3.48e-14
Threonine/Serine exporter, ThrE; ThrE_2 is a family of membrane proteins involved in the export of threonine and serine. L-threonine, L-serine are both substrates for the exporter. The exporter exhibits nine-ten predicted transmembrane-spanning helices with long charged C and N termini and an amphipathic helix present within the N terminus. L-Threonine can be made by the amino acid-producing bacterium Corynebacterium glutamicum, but the potential for amino acid formation can be considerably improved by reducing its intracellular degradation into glycine and increasing its export by this exporter. Members of the family are found in Bacteria, Archaea, and the fungal kingdoms, and the family can exist either as a single long polypeptide chain or as two short polypeptides. All family members show an extended hydrophilic N-terminal domain with weak sequence similarity to portions of hydrolases (proteases, peptidases, and glycosidases); this suggests that since this region is cytoplasmic to the membrane it may be generating the transport substrate, so may imply that threonine may not be the primary substrate and the ThrE has a subsidiary function.
Pssm-ID: 432807 Cd Length: 129 Bit Score: 68.70 E-value: 3.48e-14
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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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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(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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