Gene Ontology annotation through association of InterPro records with GO terms
Combined Automated Annotation using Multiple IEA Methods
UniProtKB record A0A0H2M1F3 (A0A0H2M1F3_VARPD) - Biopolymer transport protein ExbD from Variovorax paradoxus TBEA6
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VPARA_25800 (exbD5, A0A0H2M1F3) is a 137-aa single-pass type II inner-membrane protein containing an N-terminal transmembrane helix (residues 20-39) and a C-terminal ExbD periplasmic domain (Pfam PF02472, InterPro IPR003400, PANTHER PTHR30558).
"DR PANTHER; PTHR30558; EXBD MEMBRANE COMPONENT OF PMF-DRIVEN MACROMOLECULE IMPORT SYSTEM; 1."
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VPARA_25800 (exbD5) corresponds to EMBL CDS accession KLN56274.1 on genomic contig JZWI01000012, where consecutive CDS accessions (KLN56274.1-KLN56277.1) and locus tags stepping by 10 place exbD5 immediately upstream of exbB4 (VPARA_25810, KLN56275.1).
"DR EMBL; JZWI01000012; KLN56274.1; -; Genomic_DNA."
TonB-dependent transporters: regulation, structure, and function.
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The inner-membrane TonB-ExbB-ExbD complex harvests the proton-motive force and interacts with the periplasmic side of outer-membrane TonB-dependent receptors to drive active import of ferric-siderophore chelates.
"These transporters show high affinity and specificity for metal chelates called siderophores and require energy derived from the protonmotive force across the inner membrane to transport them (33, 87). To tap this energy source, TBDTs must interact with an inner membrane protein complex consisting of TonB, ExbB, and ExbD (72)."
Energization of Outer Membrane Transport by the ExbB ExbD Molecular Motor.
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An ExbD dimer resides within the central pore of the inner-membrane ExbB pentamer and extends into the periplasm to harvest the proton-motive force and transmit mechanical energy to TonB.
"ExbB forms a pentamer with a pore inside, in which an ExbD dimer resides. This complex harvests the energy of the pmf and transmits it to TonB."