HAMAP rule MF_00846
General rule information
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Accession | MF_00846 |
Dates | 18-NOV-2019 (Created) 17-FEB-2023 (Last updated, Version 6) |
Name | VmlR |
Scope | Bacteria; Actinomycetota
Bacteria; Bacillota
Bacteria; Mycoplasmatota |
Template | P39115 (VMLR_BACSU) |
Triggered by |
Propagated annotation
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Identifier, protein and gene names
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Identifier |
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Protein name |
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Gene name |
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Comments
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Function | Recognizes and binds in the vacant E-site of ribosomes stalled by some peptidyltransferase center (PTC)-targeting antibiotics. Makes contact with the PTC and both ribosomal subunits. Induces conformational changes in the P-site, which allows it to dislodge the antibiotic from its PTC binding site. |
Subunit | Binds within the E-site of the 70S ribosome, where it contacts ribosomal proteins of the large and small subunit, the 16 and 23S rRNAs and the acceptor arm of the P-site tRNA. |
Subcellular location | Cytoplasm. Note=Does not stably associate with ribosomes. |
Domain | The antibiotic resistance domain (ARD) is packed between the 23S rRNA and the acceptor arm of the P-site tRNA and inserts into the peptidyltransferase center (PTC). The C-terminal extension (CTE) contacts the small ribosomal subunit, positioned in the Shine-Dalgarno-anti-Shine-Dalgarno cavity. |
Similarity | Belongs to the ABC transporter superfamily. ABCF family. ARE2 subfamily. |
Keywords
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Antibiotic resistance
ATP-binding
Cytoplasm
Nucleotide-binding
Repeat
RNA-binding
rRNA-binding
tRNA-binding
ATP-binding
Cytoplasm
Nucleotide-binding
Repeat
RNA-binding
rRNA-binding
tRNA-binding
Gene Ontology
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GO:0005524; Molecular function: ATP binding.
GO:0005737; Cellular component: cytoplasm.
GO:0072344; Biological process: rescue of stalled ribosome.
GO:0019843; Molecular function: rRNA binding.
GO:0000049; Molecular function: tRNA binding.
GO:0005737; Cellular component: cytoplasm.
GO:0072344; Biological process: rescue of stalled ribosome.
GO:0019843; Molecular function: rRNA binding.
GO:0000049; Molecular function: tRNA binding.
Cross-references
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Computed features
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General | Coiled_coil; -; 0-unlimited; trigger=yes; |
Features
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From: VMLR_BACSU (P39115) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
DOMAIN | 5 | 200 | ABC transporter 1 | |||||||||
DOMAIN | 292 | 504 | ABC transporter 2 | |||||||||
BINDING | 37 | 44 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" /ligand_label="1 | G-x-N-G-[ATV]-G-K-[ST] | ||||||||
BINDING | 324 | 331 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" /ligand_label="2 | G-x-N-G-[SICA]-G-K-[TS] | ||||||||
REGION | 183 | 289 | Antibiotic resistance domain (ARD) | |||||||||
REGION | 483 | 547 | C-terminal extension (CTE) |
Additional information
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Size range | 530-560 amino acids |
Related rules | None |
Fusion | None |