30S ribosomal protein S12

Details

Name
30S ribosomal protein S12
Synonyms
  • strA
Gene Name
rpsL
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0010058|30S ribosomal protein S12
MATVNQLVRKPRARKVAKSNVPALEACPQKRGVCTRVYTTTPKKPNSALRKVCRVRLTNG
FEVTSYIGGEGHNLQEHSVILIRGGRVKDLPGVRYHTVRGALDCSGVKDRKQARSKYGVK
RPKA
Number of residues
124
Molecular Weight
13736.995
Theoretical pI
11.49
GO Classification
Functions
misfolded RNA binding / rRNA binding / structural constituent of ribosome / tRNA binding
Processes
Group I intron splicing / positive regulation of RNA splicing / response to antibiotic / RNA folding / translation
Components
cytosol / cytosolic small ribosomal subunit
General Function
Trna binding
Specific Function
With S4 and S5 plays an important role in translational accuracy.Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit (By similarity).Cryo-EM studies suggest that S12 contacts the EF-Tu bound tRNA in the A-site during codon-recognition. This contact is most likely broken as the aminoacyl-tRNA moves into the peptidyl transferase center in the 50S subunit.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasmic
Gene sequence
>lcl|BSEQ0010059|30S ribosomal protein S12 (rpsL)
ATGGCAACAGTTAACCAGCTGGTACGCAAACCACGTGCTCGCAAAGTTGCGAAAAGCAAC
GTGCCTGCGCTGGAAGCATGCCCGCAAAAACGTGGCGTATGTACTCGTGTATATACTACC
ACTCCTAAAAAACCGAACTCCGCGCTGCGTAAAGTATGCCGTGTTCGTCTGACTAACGGT
TTCGAAGTGACTTCCTACATCGGTGGTGAAGGTCACAACCTGCAGGAGCACTCCGTGATC
CTGATCCGTGGCGGTCGTGTTAAAGACCTCCCGGGTGTTCGTTACCACACCGTACGTGGT
GCGCTTGACTGCTCCGGCGTTAAAGACCGTAAGCAGGCTCGTTCCAAGTATGGCGTGAAG
CGTCCTAAGGCTTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0A7S3
UniProtKB Entry NameRS12_ECOLI
GenBank Protein ID43010
GenBank Gene IDV00355
General References
  1. Funatsu G, Yaguchi M, Wittmann-Liebold B: Primary stucture of protein S12 from the small Escherichia coli ribosomal subunit. FEBS Lett. 1977 Jan 15;73(1):12-7. [PubMed:320034]
  2. Post LE, Nomura M: DNA sequences from the str operon of Escherichia coli. J Biol Chem. 1980 May 25;255(10):4660-6. [PubMed:6989816]
  3. Timms AR, Steingrimsdottir H, Lehmann AR, Bridges BA: Mutant sequences in the rpsL gene of Escherichia coli B/r: mechanistic implications for spontaneous and ultraviolet light mutagenesis. Mol Gen Genet. 1992 Mar;232(1):89-96. [PubMed:1552908]
  4. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [PubMed:9278503]
  5. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [PubMed:16738553]
  6. Post LE, Arfsten AE, Reusser F, Nomura M: DNA sequences of promoter regions for the str and spc ribosomal protein operons in E. coli. Cell. 1978 Sep;15(1):215-29. [PubMed:151587]
  7. Urlaub H, Kruft V, Bischof O, Muller EC, Wittmann-Liebold B: Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies. EMBO J. 1995 Sep 15;14(18):4578-88. [PubMed:7556101]
  8. Allen PN, Noller HF: Mutations in ribosomal proteins S4 and S12 influence the higher order structure of 16 S ribosomal RNA. J Mol Biol. 1989 Aug 5;208(3):457-68. [PubMed:2477554]
  9. Toivonen JM, Boocock MR, Jacobs HT: Modelling in Escherichia coli of mutations in mitoribosomal protein S12: novel mutant phenotypes of rpsL. Mol Microbiol. 1999 Mar;31(6):1735-46. [PubMed:10209746]
  10. Kowalak JA, Walsh KA: Beta-methylthio-aspartic acid: identification of a novel posttranslational modification in ribosomal protein S12 from Escherichia coli. Protein Sci. 1996 Aug;5(8):1625-32. [PubMed:8844851]
  11. Arnold RJ, Reilly JP: Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry. Anal Biochem. 1999 Apr 10;269(1):105-12. [PubMed:10094780]
  12. Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y: Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli. Mol Cell Proteomics. 2009 Feb;8(2):215-25. doi: 10.1074/mcp.M800187-MCP200. Epub 2008 Aug 23. [PubMed:18723842]
  13. Valle M, Sengupta J, Swami NK, Grassucci RA, Burkhardt N, Nierhaus KH, Agrawal RK, Frank J: Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process. EMBO J. 2002 Jul 1;21(13):3557-67. [PubMed:12093756]
  14. Stark H, Rodnina MV, Wieden HJ, Zemlin F, Wintermeyer W, van Heel M: Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex. Nat Struct Biol. 2002 Nov;9(11):849-54. [PubMed:12379845]
  15. Tung CS, Joseph S, Sanbonmatsu KY: All-atom homology model of the Escherichia coli 30S ribosomal subunit. Nat Struct Biol. 2002 Oct;9(10):750-5. [PubMed:12244297]
  16. Gao H, Sengupta J, Valle M, Korostelev A, Eswar N, Stagg SM, Van Roey P, Agrawal RK, Harvey SC, Sali A, Chapman MS, Frank J: Study of the structural dynamics of the E coli 70S ribosome using real-space refinement. Cell. 2003 Jun 13;113(6):789-801. [PubMed:12809609]
  17. Schuwirth BS, Borovinskaya MA, Hau CW, Zhang W, Vila-Sanjurjo A, Holton JM, Cate JH: Structures of the bacterial ribosome at 3.5 A resolution. Science. 2005 Nov 4;310(5749):827-34. [PubMed:16272117]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00452FramycetinapprovedyesinhibitorDetails
DB00479Amikacinapproved, investigational, vet_approvedyesinhibitorDetails
DB00684Tobramycinapproved, investigationalyesinhibitorDetails
DB00798Gentamicinapproved, vet_approvedyesadductDetails
DB00919Spectinomycinapproved, investigational, vet_approvedyesinhibitorDetails
DB00955Netilmicinapproved, investigationalyesinhibitorDetails
DB00994Neomycinapproved, vet_approvedyesinhibitorDetails
DB01082Streptomycinapproved, vet_approvedyesinhibitorDetails
DB01172Kanamycinapproved, investigational, vet_approvedyesinhibitorDetails
DB03615Ribostamycinapproved, experimentalunknownDetails
DB06696Arbekacinexperimental, investigationalyesinhibitorDetails
DB04729Gentamicin C1aexperimentalyesadductDetails
DB00560TigecyclineapprovedyesadductDetails