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Protein

30S ribosomal protein S12

Gene

rpsL

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).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.

GO - Molecular functioni

  • misfolded RNA binding Source: EcoCyc
  • rRNA binding Source: EcoCyc
  • structural constituent of ribosome Source: InterPro
  • tRNA binding Source: UniProtKB-HAMAP

GO - Biological processi

  • Group I intron splicing Source: EcoCyc
  • positive regulation of RNA splicing Source: EcoCyc
  • response to antibiotic Source: UniProtKB-KW
  • RNA folding Source: EcoCyc
  • translation Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Antibiotic resistance

Keywords - Ligandi

RNA-binding, rRNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10911-MONOMER.
ECOL316407:JW3304-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S12
Gene namesi
Name:rpsL
Synonyms:strA
Ordered Locus Names:b3342, JW3304
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10911. rpsL.

Subcellular locationi

GO - Cellular componenti

  • cytosolic small ribosomal subunit Source: EcoliWiki
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi57 – 571L → H: Protein is not incorporated into ribosomes. 1 Publication
Mutagenesisi88 – 881K → Q: Confers low-level resistance to streptomycin and a 15% decrease in the translational elongation rate. 1 Publication

Chemistry

DrugBankiDB00479. Amikacin.
DB06696. Arbekacin.
DB00452. Framycetin.
DB00798. Gentamicin.
DB01172. Kanamycin.
DB00994. Neomycin.
DB00955. Netilmicin.
DB00919. Spectinomycin.
DB01082. Streptomycin.
DB00560. Tigecycline.
DB00684. Tobramycin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 12412330S ribosomal protein S12PRO_0000146219Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei89 – 8913-methylthioaspartic acid1 Publication
Modified residuei108 – 1081N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Methylation

Proteomic databases

PaxDbiP0A7S3.
PRIDEiP0A7S3.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
rimPP0A8A83EBI-543960,EBI-561065

Protein-protein interaction databases

BioGridi852156. 1 interaction.
DIPiDIP-35806N.
IntActiP0A7S3. 27 interactions.
STRINGi511145.b3342.

Structurei

Secondary structure

1
124
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 96Combined sources
Turni24 – 263Combined sources
Beta strandi30 – 367Combined sources
Beta strandi37 – 404Combined sources
Beta strandi43 – 453Combined sources
Beta strandi52 – 576Combined sources
Turni58 – 603Combined sources
Beta strandi62 – 665Combined sources
Beta strandi69 – 713Combined sources
Beta strandi79 – 846Combined sources
Beta strandi90 – 923Combined sources
Beta strandi95 – 973Combined sources
Beta strandi99 – 1013Combined sources
Turni114 – 1185Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-L2-124[»]
1MJ1electron microscopy13.00O5-123[»]
1ZN1electron microscopy14.10L28-124[»]
2YKRelectron microscopy9.80L2-124[»]
3DEGelectron microscopy-D2-124[»]
3EP2electron microscopy-L2-124[»]
3EQ3electron microscopy-L2-124[»]
3EQ4electron microscopy-L2-124[»]
3J0Delectron microscopy11.10I2-124[»]
3J0Eelectron microscopy9.90F2-124[»]
3J9Yelectron microscopy3.90l1-124[»]
4A2Ielectron microscopy16.50L2-124[»]
4ADVelectron microscopy13.50L2-124[»]
4U1UX-ray2.95AL/CL2-124[»]
4U1VX-ray3.00AL/CL2-124[»]
4U20X-ray2.90AL/CL2-124[»]
4U24X-ray2.90AL/CL2-124[»]
4U25X-ray2.90AL/CL2-124[»]
4U26X-ray2.80AL/CL2-124[»]
4U27X-ray2.80AL/CL2-124[»]
4V47electron microscopy12.30BL2-124[»]
4V48electron microscopy11.50BL2-124[»]
4V4HX-ray3.46AL/CL1-124[»]
4V4QX-ray3.46AL/CL2-124[»]
4V4Velectron microscopy15.00AL23-123[»]
4V4Welectron microscopy15.00AL23-123[»]
4V50X-ray3.22AL/CL2-124[»]
4V52X-ray3.21AL/CL2-124[»]
4V53X-ray3.54AL/CL2-124[»]
4V54X-ray3.30AL/CL2-124[»]
4V55X-ray4.00AL/CL2-124[»]
4V56X-ray3.93AL/CL2-124[»]
4V57X-ray3.50AL/CL2-124[»]
4V5BX-ray3.74BL/DL2-124[»]
4V5Helectron microscopy5.80AL2-124[»]
4V5YX-ray4.45AL/CL2-124[»]
4V64X-ray3.50AL/CL2-124[»]
4V65electron microscopy9.00AD1-124[»]
4V66electron microscopy9.00AD1-124[»]
4V69electron microscopy6.70AL2-124[»]
4V6CX-ray3.19AL/CL1-124[»]
4V6DX-ray3.81AL/CL1-124[»]
4V6EX-ray3.71AL/CL1-124[»]
4V6Kelectron microscopy8.25BP1-124[»]
4V6Lelectron microscopy13.20AP1-124[»]
4V6Melectron microscopy7.10AL2-124[»]
AO2-79[»]
AO81-89[»]
4V6Nelectron microscopy12.10BO2-124[»]
4V6Oelectron microscopy14.70AO2-124[»]
4V6Pelectron microscopy13.50AO2-124[»]
4V6Qelectron microscopy11.50AO2-124[»]
4V6Relectron microscopy11.50AO2-124[»]
4V6Selectron microscopy13.10BN2-124[»]
4V6Telectron microscopy8.30AL2-124[»]
4V6Velectron microscopy9.80AL2-124[»]
4V6Yelectron microscopy12.00AL1-124[»]
4V6Zelectron microscopy12.00AL1-124[»]
4V70electron microscopy17.00AL1-124[»]
4V71electron microscopy20.00AL1-124[»]
4V72electron microscopy13.00AL1-124[»]
4V73electron microscopy15.00AL1-124[»]
4V74electron microscopy17.00AL1-124[»]
4V75electron microscopy12.00AL1-124[»]
4V76electron microscopy17.00AL1-124[»]
4V77electron microscopy17.00AL1-124[»]
4V78electron microscopy20.00AL1-124[»]
4V79electron microscopy15.00AL1-124[»]
4V7Aelectron microscopy9.00AL1-124[»]
4V7Belectron microscopy6.80AL1-124[»]
4V7Celectron microscopy7.60AL2-124[»]
4V7Delectron microscopy7.60BL2-124[»]
4V7Ielectron microscopy9.60BL1-124[»]
4V7SX-ray3.25AL/CL2-124[»]
4V7TX-ray3.19AL/CL2-124[»]
4V7UX-ray3.10AL/CL2-124[»]
4V7VX-ray3.29AL/CL2-124[»]
4V85X-ray3.20L1-124[»]
4V89X-ray3.70AL1-124[»]
4V9CX-ray3.30AL/CL1-124[»]
4V9DX-ray3.00AL/BL2-124[»]
4V9OX-ray2.90BL/DL/FL/HL1-124[»]
4V9PX-ray2.90BL/DL/FL/HL1-124[»]
4WF1X-ray3.09AL/CL2-124[»]
4WWWX-ray3.10QL/XL2-124[»]
4YBBX-ray2.10AL/BL2-124[»]
5AFIelectron microscopy2.90l1-124[»]
DisProtiDP00145.
ProteinModelPortaliP0A7S3.
SMRiP0A7S3. Positions 2-124.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7S3.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S12P family.Curated

Phylogenomic databases

eggNOGiCOG0048.
HOGENOMiHOG000040063.
InParanoidiP0A7S3.
KOiK02950.
OMAiKSKVPAM.
OrthoDBiEOG61ZTNF.
PhylomeDBiP0A7S3.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_00403_B. Ribosomal_S12_B.
InterProiIPR012340. NA-bd_OB-fold.
IPR006032. Ribosomal_S12/S23.
IPR005679. Ribosomal_S12_bac.
[Graphical view]
PANTHERiPTHR11652. PTHR11652. 1 hit.
PfamiPF00164. Ribosom_S12_S23. 1 hit.
[Graphical view]
PIRSFiPIRSF002133. Ribosomal_S12/S23. 1 hit.
PRINTSiPR01034. RIBOSOMALS12.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00981. rpsL_bact. 1 hit.
PROSITEiPS00055. RIBOSOMAL_S12. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A7S3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATVNQLVRK PRARKVAKSN VPALEACPQK RGVCTRVYTT TPKKPNSALR
60 70 80 90 100
KVCRVRLTNG FEVTSYIGGE GHNLQEHSVI LIRGGRVKDL PGVRYHTVRG
110 120
ALDCSGVKDR KQARSKYGVK RPKA
Length:124
Mass (Da):13,737
Last modified:January 23, 2007 - v2
Checksum:i94A57F4C4FF0FC5E
GO

Mass spectrometryi

Molecular mass is 13651.3 Da from positions 2 - 124. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti43 – 431K → R Confers streptomycin resistance but not hyperaccurate translation.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS13738. R3EC12.
RefSeqiNP_417801.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC76367; AAC76367; b3342.
BAE77949; BAE77949; BAE77949.
GeneIDi947845.
KEGGiecj:Y75_p3834.
eco:b3342.
PATRICi32122116. VBIEscCol129921_3435.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS13738. R3EC12.
RefSeqiNP_417801.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-L2-124[»]
1MJ1electron microscopy13.00O5-123[»]
1ZN1electron microscopy14.10L28-124[»]
2YKRelectron microscopy9.80L2-124[»]
3DEGelectron microscopy-D2-124[»]
3EP2electron microscopy-L2-124[»]
3EQ3electron microscopy-L2-124[»]
3EQ4electron microscopy-L2-124[»]
3J0Delectron microscopy11.10I2-124[»]
3J0Eelectron microscopy9.90F2-124[»]
3J9Yelectron microscopy3.90l1-124[»]
4A2Ielectron microscopy16.50L2-124[»]
4ADVelectron microscopy13.50L2-124[»]
4U1UX-ray2.95AL/CL2-124[»]
4U1VX-ray3.00AL/CL2-124[»]
4U20X-ray2.90AL/CL2-124[»]
4U24X-ray2.90AL/CL2-124[»]
4U25X-ray2.90AL/CL2-124[»]
4U26X-ray2.80AL/CL2-124[»]
4U27X-ray2.80AL/CL2-124[»]
4V47electron microscopy12.30BL2-124[»]
4V48electron microscopy11.50BL2-124[»]
4V4HX-ray3.46AL/CL1-124[»]
4V4QX-ray3.46AL/CL2-124[»]
4V4Velectron microscopy15.00AL23-123[»]
4V4Welectron microscopy15.00AL23-123[»]
4V50X-ray3.22AL/CL2-124[»]
4V52X-ray3.21AL/CL2-124[»]
4V53X-ray3.54AL/CL2-124[»]
4V54X-ray3.30AL/CL2-124[»]
4V55X-ray4.00AL/CL2-124[»]
4V56X-ray3.93AL/CL2-124[»]
4V57X-ray3.50AL/CL2-124[»]
4V5BX-ray3.74BL/DL2-124[»]
4V5Helectron microscopy5.80AL2-124[»]
4V5YX-ray4.45AL/CL2-124[»]
4V64X-ray3.50AL/CL2-124[»]
4V65electron microscopy9.00AD1-124[»]
4V66electron microscopy9.00AD1-124[»]
4V69electron microscopy6.70AL2-124[»]
4V6CX-ray3.19AL/CL1-124[»]
4V6DX-ray3.81AL/CL1-124[»]
4V6EX-ray3.71AL/CL1-124[»]
4V6Kelectron microscopy8.25BP1-124[»]
4V6Lelectron microscopy13.20AP1-124[»]
4V6Melectron microscopy7.10AL2-124[»]
AO2-79[»]
AO81-89[»]
4V6Nelectron microscopy12.10BO2-124[»]
4V6Oelectron microscopy14.70AO2-124[»]
4V6Pelectron microscopy13.50AO2-124[»]
4V6Qelectron microscopy11.50AO2-124[»]
4V6Relectron microscopy11.50AO2-124[»]
4V6Selectron microscopy13.10BN2-124[»]
4V6Telectron microscopy8.30AL2-124[»]
4V6Velectron microscopy9.80AL2-124[»]
4V6Yelectron microscopy12.00AL1-124[»]
4V6Zelectron microscopy12.00AL1-124[»]
4V70electron microscopy17.00AL1-124[»]
4V71electron microscopy20.00AL1-124[»]
4V72electron microscopy13.00AL1-124[»]
4V73electron microscopy15.00AL1-124[»]
4V74electron microscopy17.00AL1-124[»]
4V75electron microscopy12.00AL1-124[»]
4V76electron microscopy17.00AL1-124[»]
4V77electron microscopy17.00AL1-124[»]
4V78electron microscopy20.00AL1-124[»]
4V79electron microscopy15.00AL1-124[»]
4V7Aelectron microscopy9.00AL1-124[»]
4V7Belectron microscopy6.80AL1-124[»]
4V7Celectron microscopy7.60AL2-124[»]
4V7Delectron microscopy7.60BL2-124[»]
4V7Ielectron microscopy9.60BL1-124[»]
4V7SX-ray3.25AL/CL2-124[»]
4V7TX-ray3.19AL/CL2-124[»]
4V7UX-ray3.10AL/CL2-124[»]
4V7VX-ray3.29AL/CL2-124[»]
4V85X-ray3.20L1-124[»]
4V89X-ray3.70AL1-124[»]
4V9CX-ray3.30AL/CL1-124[»]
4V9DX-ray3.00AL/BL2-124[»]
4V9OX-ray2.90BL/DL/FL/HL1-124[»]
4V9PX-ray2.90BL/DL/FL/HL1-124[»]
4WF1X-ray3.09AL/CL2-124[»]
4WWWX-ray3.10QL/XL2-124[»]
4YBBX-ray2.10AL/BL2-124[»]
5AFIelectron microscopy2.90l1-124[»]
DisProtiDP00145.
ProteinModelPortaliP0A7S3.
SMRiP0A7S3. Positions 2-124.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi852156. 1 interaction.
DIPiDIP-35806N.
IntActiP0A7S3. 27 interactions.
STRINGi511145.b3342.

Chemistry

ChEMBLiCHEMBL2363135.
DrugBankiDB00479. Amikacin.
DB06696. Arbekacin.
DB00452. Framycetin.
DB00798. Gentamicin.
DB01172. Kanamycin.
DB00994. Neomycin.
DB00955. Netilmicin.
DB00919. Spectinomycin.
DB01082. Streptomycin.
DB00560. Tigecycline.
DB00684. Tobramycin.

Proteomic databases

PaxDbiP0A7S3.
PRIDEiP0A7S3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76367; AAC76367; b3342.
BAE77949; BAE77949; BAE77949.
GeneIDi947845.
KEGGiecj:Y75_p3834.
eco:b3342.
PATRICi32122116. VBIEscCol129921_3435.

Organism-specific databases

EchoBASEiEB0904.
EcoGeneiEG10911. rpsL.

Phylogenomic databases

eggNOGiCOG0048.
HOGENOMiHOG000040063.
InParanoidiP0A7S3.
KOiK02950.
OMAiKSKVPAM.
OrthoDBiEOG61ZTNF.
PhylomeDBiP0A7S3.

Enzyme and pathway databases

BioCyciEcoCyc:EG10911-MONOMER.
ECOL316407:JW3304-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7S3.
PROiP0A7S3.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_00403_B. Ribosomal_S12_B.
InterProiIPR012340. NA-bd_OB-fold.
IPR006032. Ribosomal_S12/S23.
IPR005679. Ribosomal_S12_bac.
[Graphical view]
PANTHERiPTHR11652. PTHR11652. 1 hit.
PfamiPF00164. Ribosom_S12_S23. 1 hit.
[Graphical view]
PIRSFiPIRSF002133. Ribosomal_S12/S23. 1 hit.
PRINTSiPR01034. RIBOSOMALS12.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00981. rpsL_bact. 1 hit.
PROSITEiPS00055. RIBOSOMAL_S12. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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: 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. 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.

Entry informationi

Entry nameiRS12_ECOLI
AccessioniPrimary (citable) accession number: P0A7S3
Secondary accession number(s): P02367, Q2M707, Q9F5N3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.