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P0A7S3 (RS12_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
30S ribosomal protein S12
Gene names
Name:rpsL
Synonyms:strA
Ordered Locus Names:b3342, JW3304
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length124 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

With S4 and S5 plays an important role in translational accuracy. HAMAP-Rule MF_00403_B

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. HAMAP-Rule MF_00403_B

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. HAMAP-Rule MF_00403_B

Subunit structure

Part of the 30S ribosomal subunit. Contacts proteins S8 and S17. May interact with IF1 in the 30S initiation complex By similarity.

Miscellaneous

At least 19 substitutions or deletions in 11 codons can promote streptomycin resistance, dependence or pseudodependence; all but one of the streptomycin resistant mutations (K42R) are associated with hyperaccurate translation and thus reduced translational efficiency.

The streptomycin sensitive allele is dominant to resistant alleles.

Sequence similarities

Belongs to the ribosomal protein S12P family.

Mass spectrometry

Molecular mass is 13651.3 Da from positions 2 - 124. Determined by MALDI. Ref.12

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.8
Chain2 – 12412330S ribosomal protein S12 HAMAP-Rule MF_00403_B
PRO_0000146219

Amino acid modifications

Modified residue8913-methylthioaspartic acid HAMAP-Rule MF_00403_B
Modified residue1081N6-acetyllysine Ref.13

Natural variations

Natural variant431K → R Confers streptomycin resistance but not hyperaccurate translation.

Experimental info

Mutagenesis571L → H: Protein is not incorporated into ribosomes. Ref.10
Mutagenesis881K → Q: Confers low-level resistance to streptomycin and a 15% decrease in the translational elongation rate. Ref.10

Secondary structure

............................ 124
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7S3 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 94A57F4C4FF0FC5E

FASTA12413,737
        10         20         30         40         50         60 
MATVNQLVRK PRARKVAKSN VPALEACPQK RGVCTRVYTT TPKKPNSALR KVCRVRLTNG 

        70         80         90        100        110        120 
FEVTSYIGGE GHNLQEHSVI LIRGGRVKDL PGVRYHTVRG ALDCSGVKDR KQARSKYGVK 


RPKA 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure of protein S12 from the small Escherichia coli ribosomal subunit."
Funatsu G., Yaguchi M., Wittmann-Liebold B.
FEBS Lett. 73:12-17(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-124.
Strain: K.
[2]"DNA sequences from the str operon of Escherichia coli."
Post L.E., Nomura M.
J. Biol. Chem. 255:4660-4666(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[3]"Mutant sequences in the rpsL gene of Escherichia coli B/r: mechanistic implications for spontaneous and ultraviolet light mutagenesis."
Timms A.R., Steingrimsdottir H., Lehmann A.R., Bridges B.A.
Mol. Gen. Genet. 232:89-96(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS STREPTOMYCIN RESISTANT.
Strain: B/R WP2.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Nucleotide information of the rpsL150 allele of MC4100, strain of Escherichia coli."
Kharat A.S., Blot M.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT STREPTOMYCIN RESISTANT.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574 and K12 / W3110 / ZK126.
[6]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]"DNA sequences of promoter regions for the str and spc ribosomal protein operons in E. coli."
Post L.E., Arfsten A.E., Reusser F., Nomura M.
Cell 15:215-229(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
Strain: K12.
[8]"Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies."
Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.
EMBO J. 14:4578-4588(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-11, CROSS-LINKING TO RRNA.
Strain: MRE-600.
[9]"Mutations in ribosomal proteins S4 and S12 influence the higher order structure of 16 S ribosomal RNA."
Allen P.N., Noller H.F.
J. Mol. Biol. 208:457-468(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: EFFECT OF MUTATIONS ON RRNA FOLDING.
Strain: UD1A1.
[10]"Modelling in Escherichia coli of mutations in mitoribosomal protein S12: novel mutant phenotypes of rpsL."
Toivonen J.M., Boocock M.R., Jacobs H.T.
Mol. Microbiol. 31:1735-1746(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LEU-57 AND LYS-88.
Strain: K12.
[11]"Beta-methylthio-aspartic acid: identification of a novel posttranslational modification in ribosomal protein S12 from Escherichia coli."
Kowalak J.A., Walsh K.A.
Protein Sci. 5:1625-1632(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: BETA-METHYLTHIOLATION AT ASP-89.
[12]"Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry."
Arnold R.J., Reilly J.P.
Anal. Biochem. 269:105-112(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MASS SPECTROMETRY.
Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
[13]"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-108, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[14]"Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process."
Valle M., Sengupta J., Swami N.K., Grassucci R.A., Burkhardt N., Nierhaus K.H., Agrawal R.K., Frank J.
EMBO J. 21:3557-3567(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11 ANGSTROMS) OF KIRROMYCIN-STALLED RIBOSOMES COMPLEXED WITH EF-TU/AMINOACYL-TRNA/GTP.
[15]"Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex."
Stark H., Rodnina M.V., Wieden H.-J., Zemlin F., Wintermeyer W., Van Heel M.
Nat. Struct. Biol. 9:849-854(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (13 ANGSTROMS) OF KIRROMYCIN-STALLED RIBOSOMES COMPLEXED WITH EF-TU/AMINOACYL-TRNA/GTP.
Strain: MRE-600.
[16]"All-atom homology model of the Escherichia coli 30S ribosomal subunit."
Tung C.-S., Joseph S., Sanbonmatsu K.Y.
Nat. Struct. Biol. 9:750-755(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[17]"Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement."
Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J.
Cell 113:789-801(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS).
Strain: MRE-600.
[18]"Structures of the bacterial ribosome at 3.5 A resolution."
Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W., Vila-Sanjurjo A., Holton J.M., Cate J.H.D.
Science 310:827-834(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
Strain: MRE-600.
[19]"Limitations of translational accuracy."
Kurland C.G., Hughes D., Ehrenberg M.
(In) Neidhardt F.C., Curtiss R. III, Ingraham J.L., Lin E.C.C., Low K.B. Magasanik B., Reznikoff W.S., Riley M., Schaechter M., Umbarger H.E. (eds.); Escherichia coli and Salmonella: Cellular and molecular biology (2nd ed.), pp.979-1004, American Society for Microbiology Press, Washington D.C. (1996)
Cited for: REVIEW ON TRANSLATIONAL ACCURACY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00355 Genomic DNA. Translation: CAA23648.1.
U18997 Genomic DNA. Translation: AAA58139.1.
U00096 Genomic DNA. Translation: AAC76367.1.
AP009048 Genomic DNA. Translation: BAE77949.1.
AF312716 Genomic DNA. Translation: AAG30936.1.
AF312717 Genomic DNA. Translation: AAG30937.1.
V00354 Genomic DNA. Translation: CAA23647.1.
J01688 Genomic DNA. Translation: AAA50988.1.
PIRR3EC12. S13738.
RefSeqNP_417801.1. NC_000913.3.
YP_492090.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-L2-124[»]
1MJ1electron microscopy13.00O5-123[»]
1P6Gelectron microscopy12.30L2-124[»]
1P87electron microscopy11.50L2-124[»]
1VS5X-ray3.46L1-124[»]
1VS7X-ray3.46L1-124[»]
1ZN1electron microscopy14.10L28-123[»]
2AVYX-ray3.46L2-124[»]
2AW7X-ray3.46L2-124[»]
2GY9electron microscopy15.00L23-122[»]
2GYBelectron microscopy15.00L23-122[»]
2I2PX-ray3.22L2-123[»]
2I2UX-ray3.22L2-123[»]
2QALX-ray3.21L2-124[»]
2QANX-ray3.21L2-124[»]
2QB9X-ray3.54L2-124[»]
2QBBX-ray3.54L2-124[»]
2QBDX-ray3.30L2-124[»]
2QBFX-ray3.30L2-124[»]
2QBHX-ray4.00L2-124[»]
2QBJX-ray4.00L2-124[»]
2QOUX-ray3.93L2-124[»]
2QOWX-ray3.93L2-124[»]
2QOYX-ray3.50L2-124[»]
2QP0X-ray3.50L2-124[»]
2VHOX-ray3.74L2-124[»]
2VHPX-ray3.74L2-124[»]
2WWLelectron microscopy5.80L2-124[»]
2YKRelectron microscopy9.80L2-124[»]
2Z4KX-ray4.45L2-124[»]
2Z4MX-ray4.45L2-124[»]
3DEGelectron microscopy-D2-124[»]
3DF1X-ray3.50L2-123[»]
3DF3X-ray3.50L2-123[»]
3E1Aelectron microscopy-D1-124[»]
3E1Celectron microscopy-D1-124[»]
3EP2electron microscopy-L2-124[»]
3EQ3electron microscopy-L2-124[»]
3EQ4electron microscopy-L2-124[»]
3FIHelectron microscopy6.70L2-124[»]
3I1MX-ray3.19L1-124[»]
3I1OX-ray3.19L1-124[»]
3I1QX-ray3.81L1-124[»]
3I1SX-ray3.81L1-124[»]
3I1ZX-ray3.71L1-124[»]
3I21X-ray3.71L1-124[»]
3IZVelectron microscopy-P1-124[»]
3IZWelectron microscopy-P1-124[»]
3J00electron microscopy-L2-124[»]
3J0Delectron microscopy11.10I2-124[»]
3J0Eelectron microscopy9.90F2-124[»]
3J0Uelectron microscopy12.10O2-124[»]
3J0Velectron microscopy14.70O2-124[»]
3J0Xelectron microscopy13.50O2-124[»]
3J0Zelectron microscopy11.50O2-124[»]
3J10electron microscopy11.50O2-124[»]
3J13electron microscopy13.10N2-124[»]
3J18electron microscopy8.30L2-124[»]
3J36electron microscopy9.80L2-124[»]
3J4Velectron microscopy12.00L1-124[»]
3J4Welectron microscopy12.00L1-124[»]
3J4Yelectron microscopy17.00L1-124[»]
3J4Zelectron microscopy20.00L1-124[»]
3J53electron microscopy13.00L1-124[»]
3J55electron microscopy15.00L1-124[»]
3J57electron microscopy17.00L1-124[»]
3J59electron microscopy12.00L1-124[»]
3J5Belectron microscopy17.00L1-124[»]
3J5Delectron microscopy17.00L1-124[»]
3J5Felectron microscopy20.00L1-124[»]
3J5Helectron microscopy15.00L1-124[»]
3J5Jelectron microscopy9.00L1-124[»]
3J5Nelectron microscopy6.80L1-124[»]
3J5Telectron microscopy7.60L2-124[»]
3J5Xelectron microscopy7.60L2-124[»]
3KC4electron microscopy-L1-124[»]
3OAQX-ray3.25L2-124[»]
3OARX-ray3.25L2-124[»]
3OFAX-ray3.19L2-124[»]
3OFBX-ray3.19L2-124[»]
3OFOX-ray3.10L2-124[»]
3OFPX-ray3.10L2-124[»]
3OFXX-ray3.29L2-124[»]
3OFYX-ray3.29L2-124[»]
3OR9X-ray3.30L1-124[»]
3ORAX-ray3.30L1-124[»]
3SFSX-ray3.20L1-124[»]
3UOQX-ray3.70L1-124[»]
4A2Ielectron microscopy16.50L2-124[»]
4ADVelectron microscopy13.50L2-124[»]
4GAQX-ray3.30L1-124[»]
4GASX-ray3.30L1-124[»]
4GD1X-ray3.00L2-124[»]
4GD2X-ray3.00L2-124[»]
4KIYX-ray2.90L1-124[»]
4KJ0X-ray2.90L1-124[»]
4KJ2X-ray2.90L1-124[»]
4KJ4X-ray2.90L1-124[»]
4KJ6X-ray2.90L1-124[»]
4KJ8X-ray2.90L1-124[»]
4KJAX-ray2.90L1-124[»]
4KJCX-ray2.90L1-124[»]
DisProtDP00145.
ProteinModelPortalP0A7S3.
SMRP0A7S3. Positions 2-124.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid852156. 1 interaction.
DIPDIP-35806N.
IntActP0A7S3. 26 interactions.
STRING511145.b3342.

Chemistry

ChEMBLCHEMBL2363135.
DrugBankDB00479. Amikacin.
DB00452. Framycetin.
DB00798. Gentamicin.
DB01172. Kanamycin.
DB00994. Neomycin.
DB00955. Netilmicin.
DB00919. Spectinomycin.
DB01082. Streptomycin.
DB00684. Tobramycin.

Proteomic databases

PaxDbP0A7S3.
PRIDEP0A7S3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76367; AAC76367; b3342.
BAE77949; BAE77949; BAE77949.
GeneID12932620.
947845.
KEGGecj:Y75_p3834.
eco:b3342.
PATRIC32122116. VBIEscCol129921_3435.

Organism-specific databases

EchoBASEEB0904.
EcoGeneEG10911. rpsL.

Phylogenomic databases

eggNOGCOG0048.
HOGENOMHOG000040063.
KOK02950.
OMAKSKVPAM.
OrthoDBEOG61ZTNF.
PhylomeDBP0A7S3.
ProtClustDBPRK05163.

Enzyme and pathway databases

BioCycEcoCyc:EG10911-MONOMER.
ECOL316407:JW3304-MONOMER.

Gene expression databases

GenevestigatorP0A7S3.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
HAMAPMF_00403_B. Ribosomal_S12_B.
InterProIPR012340. NA-bd_OB-fold.
IPR006032. Ribosomal_S12/S23.
IPR005679. Ribosomal_S12_bac.
[Graphical view]
PANTHERPTHR11652. PTHR11652. 1 hit.
PfamPF00164. Ribosom_S12_S23. 1 hit.
[Graphical view]
PIRSFPIRSF002133. Ribosomal_S12/S23. 1 hit.
PRINTSPR01034. RIBOSOMALS12.
SUPFAMSSF50249. SSF50249. 1 hit.
TIGRFAMsTIGR00981. rpsL_bact. 1 hit.
PROSITEPS00055. RIBOSOMAL_S12. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A7S3.
PROP0A7S3.

Entry information

Entry nameRS12_ECOLI
AccessionPrimary (citable) accession number: P0A7S3
Secondary accession number(s): P02367, Q2M707, Q9F5N3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene