Detail Information for IndEnz0002008718
IED ID IndEnz0002008718
Enzyme Type ID protease008718
Protein Name 50S ribosomal protein L31
Large ribosomal subunit protein bL31-A
Gene Name rpmE b3936 JW3907
Organism Escherichia coli (strain K12)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12)
Enzyme Sequence MKKDIHPKYEEITASCSCGNVMKIRSTVGHDLNLDVCSKCHPFFTGKQRDVATGGRVDRFNKRFNIPGSK
Enzyme Length 70
Uniprot Accession Number P0A7M9
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Binds the 23S rRNA. {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (2); Chain (1); Metal binding (1); Modified residue (1); Mutagenesis (3)
Keywords 3D-structure;Acetylation;Direct protein sequencing;Metal-binding;RNA-binding;Reference proteome;Ribonucleoprotein;Ribosomal protein;Zinc;rRNA-binding
Interact With
Induction
Subcellular Location
Modified Residue MOD_RES 8; /note=N6-acetyllysine; /evidence=ECO:0000269|PubMed:18723842
Post Translational Modification PTM: Proteolytically cleaved by protease VII to yield a peptide lacking residues 63-70. It is not clear if this is due to protein degradation or is a bona fide processing event in the strain used in PubMed:339950 and PubMed:10556732. In strains B, D10, MRE-600 and Q13 the only protein seen in PubMed:10556732 was full-length; the last 7 amino acids were sequenced only for strain MRE-600. {ECO:0000269|PubMed:10556732, ECO:0000269|PubMed:339950}.
Signal Peptide
Structure 3D Electron microscopy (103); X-ray crystallography (4)
Cross Reference PDB 2J28; 2RDO; 3BBX; 3J9Y; 3J9Z; 3JA1; 4V4H; 4V4Q; 4V5B; 4V65; 4V66; 4V6K; 4V6L; 4V6N; 4V6O; 4V6P; 4V6Q; 4V6R; 4V6S; 4V6V; 5AFI; 5AKA; 5IQR; 5KCS; 5KPS; 5KPV; 5KPW; 5KPX; 5L3P; 5LZA; 5LZB; 5LZC; 5LZD; 5LZE; 5LZF; 5MDV; 5MDW; 5MDY; 5MDZ; 5MGP; 5NP6; 5NWY; 5O2R; 5U9F; 5U9G; 5UYK; 5UYL; 5UYM; 5UYN; 5UYP; 5UYQ; 5WDT; 5WE4; 5WE6; 5WFK; 6BU8; 6BY1; 6C4I; 6ENF; 6ENJ; 6ENU; 6H4N; 6H58; 6HRM; 6O9J; 6ORE; 6OT3; 6OUO; 6Q97; 6Q98; 6Q9A; 6SZS; 6TBV; 6TC3; 6WNT; 6WNV; 6WNW; 6Y69; 7AC7; 7ACJ; 7ACR; 7B5K; 7BL2; 7BL3; 7BL4; 7BL5; 7BL6; 7D6Z; 7K50; 7K51; 7K52; 7K53; 7K54; 7K55; 7LV0; 7N1P; 7N2C; 7N2U; 7N2V; 7N30; 7N31; 7O19; 7O1A; 7O1C; 7P3K; 7PJV; 7PJY;
Mapped Pubmed ID 16606699; 16998486; 17086193; 17996252; 18288106; 19013177; 21378755; 22467828; 23403578; 24561554; 25707802; 25775537; 25870267; 26229983; 27226493; 27279228; 27330110; 27434674; 27842381; 28300532; 28538735; 28556777; 28630923; 28741611; 29100052; 29247757; 29403017; 29733411; 30177741; 30518861; 30552154; 30765567; 31108498; 31189921; 31776341; 32094585; 32518240; 32601485; 33639093; 33761323; 34234344; 34330903; 34389707; 34403461; 34504068; 34635670; 7026537;
Motif
Gene Encoded By
Mass 7,871
Kinetics
Metal Binding METAL 16; /note=Zinc; /evidence=ECO:0000305
Rhea ID
Cross Reference Brenda