Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | 30S ribosomal protein S19 |
Protein Synonyms/Alias | |
Gene Name | rpsS |
Gene Synonyms/Alias | b3316, JW3278 |
Created Date | 3-June-2014 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Phosphorylation | Position | Peptide | Code | Type | References | 35 | KKPLRTWSRRSTIFP | S | HTP | [1] | 39 | RTWSRRSTIFPNMIG | T | HTP | [1] | 33 | GDKKPLRTWSRRSTI | T | HTP | [1] | 38 | LRTWSRRSTIFPNMI | S | HTP | [1] | |
Reference | [1]The Escherichia coli phosphotyrosine proteome relates to core pathways and virulence. Hansen AM,Chaerkady R,Sharma J,Díaz-Mejía JJ,Tyagi N,Renuse S,Jacob HK,Pinto SM,Sahasrabuddhe NA,Kim MS,Delanghe B,Srinivasan N,Emili A,Kaper JB,Pandey A PLoS Pathog. 2013;9(6):e1003403. [ PMID:23785281] |
Functional Description From UniProt | FUNCTION: In the E.coli 70S ribosome in the initiation state (PubMed:12809609) it has been modeled to contact the 23S rRNA of the 50S subunit forming part of bridge B1a; this bridge is broken in the model with bound EF-G. The 23S rRNA contact site in bridge B1a is modeled to differ in different ribosomal states (PubMed:12859903), contacting alternately S13 or S19. In the 3.5 angstroms resolved ribosome structures (PubMed:16272117) the contacts between L5, S13 and S19 bridge B1b are different, confirming the dynamic nature of this interaction. Bridge B1a is not visible in the crystallized ribosomes due to 23S rRNA disorder |
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| 3D-structure; Completeproteome; Directproteinsequencing; Referenceproteome; Ribonucleoprotein; Ribosomalprotein; RNA-binding; rRNA-binding; tRNA-binding |
Protein Sequence | MPRSLKKGPF IDLHLLKKVE KAVESGDKKP LRTWSRRSTI FPNMIGLTIA VHNGRQHVPV 60 FVTDEMVGHK LGEFAPTRTY RGHAADKKAK KK 92 |
| GO:0022627 C:cytosolic small ribosomal subunit IDA:EcoCyc GO:0019843 F:rRNA binding IEA:UniProtKB-HAMAP GO:0003735 F:structural constituent of ribosome IEA:InterPro GO:0000049 F:tRNA binding IEA:UniProtKB-KW GO:0006412 P:translation IEA:UniProtKB-HAMAP |
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