HAMAP rule MF_01552
General rule information
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| Accession | MF_01552 |
| Dates | 30-NOV-2005 (Created)
1-JUN-2023 (Last updated, Version 25) |
| Name | RimK |
| Scope(s) |
Bacteria Cyanobacteriota Planctomycetota Pseudomonadota Archaea Methanomicrobia |
| Template(s) | P0C0U4 (RIMK_ECOLI); [ Recover all ] |
| Triggered by |
HAMAP; MF_01552 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | RIMK |
| case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella> | |
| Protein name | RecName: Full=Ribosomal protein bS6--L-glutamate ligase; EC=6.3.2.-; AltName: Full=Poly-alpha-glutamate synthase; AltName: Full=Ribosomal protein bS6 modification protein; |
| else | |
| Protein name | RecName: Full=Probable alpha-L-glutamate ligase; EC=6.3.2.-; |
| end case | |
| Gene name | Name=rimK; |
Comments
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| case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella> | |
| FUNCTION | An L-glutamate ligase that catalyzes the ATP-dependent post- translational addition of glutamate residues to the C-terminus of ribosomal protein bS6 (RpsF). Is also able to catalyze the synthesis of poly-alpha-glutamate in vitro, via ATP hydrolysis from unprotected glutamate as substrate. The number of glutamate residues added to either RpsF or to poly-alpha-glutamate changes with pH. |
| end case | |
| case <FTGroup:1> | |
| COFACTOR | Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Note=Binds 2 magnesium or manganese ions per subunit.; |
| end case | |
| SIMILARITY | Belongs to the RimK family. |
Keywords
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| ATP-binding | |
| Ligase | |
| Nucleotide-binding | |
| Protein biosynthesis | |
| case <FTGroup:1> | |
| Magnesium | |
| Manganese | |
| Metal-binding | |
| end case | |
Gene Ontology
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| GO:0005524; Molecular function:ATP binding | |
| case <OCellular component:Escherichia> or <OC:Shigella> or <OC:Salmonella> | |
| GO:0018169; Molecular function:ribosomal S6-glutamic acid ligase activity | |
| GO:0018410; Biological process:C-terminal protein amino acid modification | |
| else; https://www.ebi.ac.uk/QuickGO/term/else | |
| GO:0016881; Molecular function:acid-amino acid ligase activity | |
| end case | |
Cross-references
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Features
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| From: RIMK_ECOLI (P0C0U4) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 178 | 179 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
[EDQ]-[YF] | ||||||||
| BINDING | 211 | 213 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
R-[SA]-N | ||||||||
| BINDING | 248 | 248 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="1" |
D | 1 | |||||||
| BINDING | 248 | 248 | /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="1" |
D | 1 | |||||||
| BINDING | 260 | 260 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="1" |
E | 1 | |||||||
| BINDING | 260 | 260 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2" |
E | 1 | |||||||
| BINDING | 260 | 260 | /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="1" |
E | 1 | |||||||
| BINDING | 260 | 260 | /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="2" |
E | 1 | |||||||
| BINDING | 262 | 262 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2" |
N | 1 | |||||||
| BINDING | 262 | 262 | /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="2" |
N | 1 | |||||||
| BINDING | 141 | 141 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
K | ||||||||
| BINDING | 187 | 187 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
D | ||||||||
Additional information
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| Size range | 291-313 amino acids |
| Related rules |
None |
| Fusion | Nter: <Unknown> Cter: None |
| Comments | The ribosomal protein bS6-modifying function does not apply to all RimK family members since some bacteria do not possess a rpsF gene in their genome, or the C-terminal sequence of RpsF is not conserved, or does not end with a glutamate residue. |