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P0A7S3

- RS12_ECOLI

UniProt

P0A7S3 - RS12_ECOLI

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Protein
30S ribosomal protein S12
Gene
rpsL, strA, b3342, JW3304
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

With S4 and S5 plays an important role in translational accuracy.UniRule annotation
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.UniRule annotation
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.UniRule annotation

GO - Molecular functioni

  1. misfolded RNA binding Source: EcoCyc
  2. protein binding Source: IntAct
  3. rRNA binding Source: EcoCyc
  4. structural constituent of ribosome Source: InterPro
  5. tRNA binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. Group I intron splicing Source: EcoCyc
  2. RNA folding Source: EcoCyc
  3. positive regulation of RNA splicing Source: EcoCyc
  4. response to antibiotic Source: UniProtKB-KW
  5. 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: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10911. rpsL.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic small ribosomal subunit Source: EcoCyc
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 12412330S ribosomal protein S12UniRule annotation
PRO_0000146219Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0A7S3.
PRIDEiP0A7S3.

Expressioni

Gene expression databases

GenevestigatoriP0A7S3.

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.

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

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 96
Turni24 – 263
Beta strandi30 – 323
Beta strandi36 – 405
Beta strandi43 – 453
Beta strandi50 – 578
Turni58 – 603
Beta strandi62 – 665
Beta strandi69 – 713
Beta strandi80 – 823
Beta strandi88 – 903
Beta strandi95 – 973
Beta strandi99 – 1013
Turni114 – 1185

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 microscopy14.10L28-124[»]
2AVYX-ray3.46L2-124[»]
2AW7X-ray3.46L2-124[»]
2GY9electron microscopy15.00L23-123[»]
2GYBelectron microscopy15.00L23-123[»]
2I2PX-ray3.22L2-124[»]
2I2UX-ray3.22L2-124[»]
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[»]
DisProtiDP00145.
ProteinModelPortaliP0A7S3.
SMRiP0A7S3. Positions 2-124.

Miscellaneous databases

EvolutionaryTraceiP0A7S3.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0048.
HOGENOMiHOG000040063.
KOiK02950.
OMAiCYQRKGV.
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

MATVNQLVRK PRARKVAKSN VPALEACPQK RGVCTRVYTT TPKKPNSALR    50
KVCRVRLTNG FEVTSYIGGE GHNLQEHSVI LIRGGRVKDL PGVRYHTVRG 100
ALDCSGVKDR KQARSKYGVK RPKA 124
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:
EMBL
GenBank
DDBJ
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.
YP_492090.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76367; AAC76367; b3342.
BAE77949; BAE77949; BAE77949.
GeneIDi12932620.
947845.
KEGGiecj:Y75_p3834.
eco:b3342.
PATRICi32122116. VBIEscCol129921_3435.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi S13738. R3EC12.
RefSeqi NP_417801.1. NC_000913.3.
YP_492090.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1M5G model - L 2-124 [» ]
1MJ1 electron microscopy 13.00 O 5-123 [» ]
1P6G electron microscopy 12.30 L 2-124 [» ]
1P87 electron microscopy 11.50 L 2-124 [» ]
1VS5 X-ray 3.46 L 1-124 [» ]
1VS7 X-ray 3.46 L 1-124 [» ]
1ZN1 electron microscopy 14.10 L 28-124 [» ]
2AVY X-ray 3.46 L 2-124 [» ]
2AW7 X-ray 3.46 L 2-124 [» ]
2GY9 electron microscopy 15.00 L 23-123 [» ]
2GYB electron microscopy 15.00 L 23-123 [» ]
2I2P X-ray 3.22 L 2-124 [» ]
2I2U X-ray 3.22 L 2-124 [» ]
2QAL X-ray 3.21 L 2-124 [» ]
2QAN X-ray 3.21 L 2-124 [» ]
2QB9 X-ray 3.54 L 2-124 [» ]
2QBB X-ray 3.54 L 2-124 [» ]
2QBD X-ray 3.30 L 2-124 [» ]
2QBF X-ray 3.30 L 2-124 [» ]
2QBH X-ray 4.00 L 2-124 [» ]
2QBJ X-ray 4.00 L 2-124 [» ]
2QOU X-ray 3.93 L 2-124 [» ]
2QOW X-ray 3.93 L 2-124 [» ]
2QOY X-ray 3.50 L 2-124 [» ]
2QP0 X-ray 3.50 L 2-124 [» ]
2VHO X-ray 3.74 L 2-124 [» ]
2VHP X-ray 3.74 L 2-124 [» ]
2WWL electron microscopy 5.80 L 2-124 [» ]
2YKR electron microscopy 9.80 L 2-124 [» ]
2Z4K X-ray 4.45 L 2-124 [» ]
2Z4M X-ray 4.45 L 2-124 [» ]
3DEG electron microscopy - D 2-124 [» ]
3DF1 X-ray 3.50 L 2-123 [» ]
3DF3 X-ray 3.50 L 2-123 [» ]
3E1A electron microscopy - D 1-124 [» ]
3E1C electron microscopy - D 1-124 [» ]
3EP2 electron microscopy - L 2-124 [» ]
3EQ3 electron microscopy - L 2-124 [» ]
3EQ4 electron microscopy - L 2-124 [» ]
3FIH electron microscopy 6.70 L 2-124 [» ]
3I1M X-ray 3.19 L 1-124 [» ]
3I1O X-ray 3.19 L 1-124 [» ]
3I1Q X-ray 3.81 L 1-124 [» ]
3I1S X-ray 3.81 L 1-124 [» ]
3I1Z X-ray 3.71 L 1-124 [» ]
3I21 X-ray 3.71 L 1-124 [» ]
3IZV electron microscopy - P 1-124 [» ]
3IZW electron microscopy - P 1-124 [» ]
3J00 electron microscopy - L 2-124 [» ]
3J0D electron microscopy 11.10 I 2-124 [» ]
3J0E electron microscopy 9.90 F 2-124 [» ]
3J0U electron microscopy 12.10 O 2-124 [» ]
3J0V electron microscopy 14.70 O 2-124 [» ]
3J0X electron microscopy 13.50 O 2-124 [» ]
3J0Z electron microscopy 11.50 O 2-124 [» ]
3J10 electron microscopy 11.50 O 2-124 [» ]
3J13 electron microscopy 13.10 N 2-124 [» ]
3J18 electron microscopy 8.30 L 2-124 [» ]
3J36 electron microscopy 9.80 L 2-124 [» ]
3J4V electron microscopy 12.00 L 1-124 [» ]
3J4W electron microscopy 12.00 L 1-124 [» ]
3J4Y electron microscopy 17.00 L 1-124 [» ]
3J4Z electron microscopy 20.00 L 1-124 [» ]
3J53 electron microscopy 13.00 L 1-124 [» ]
3J55 electron microscopy 15.00 L 1-124 [» ]
3J57 electron microscopy 17.00 L 1-124 [» ]
3J59 electron microscopy 12.00 L 1-124 [» ]
3J5B electron microscopy 17.00 L 1-124 [» ]
3J5D electron microscopy 17.00 L 1-124 [» ]
3J5F electron microscopy 20.00 L 1-124 [» ]
3J5H electron microscopy 15.00 L 1-124 [» ]
3J5J electron microscopy 9.00 L 1-124 [» ]
3J5N electron microscopy 6.80 L 1-124 [» ]
3J5T electron microscopy 7.60 L 2-124 [» ]
3J5X electron microscopy 7.60 L 2-124 [» ]
3KC4 electron microscopy - L 1-124 [» ]
3OAQ X-ray 3.25 L 2-124 [» ]
3OAR X-ray 3.25 L 2-124 [» ]
3OFA X-ray 3.19 L 2-124 [» ]
3OFB X-ray 3.19 L 2-124 [» ]
3OFO X-ray 3.10 L 2-124 [» ]
3OFP X-ray 3.10 L 2-124 [» ]
3OFX X-ray 3.29 L 2-124 [» ]
3OFY X-ray 3.29 L 2-124 [» ]
3OR9 X-ray 3.30 L 1-124 [» ]
3ORA X-ray 3.30 L 1-124 [» ]
3SFS X-ray 3.20 L 1-124 [» ]
3UOQ X-ray 3.70 L 1-124 [» ]
4A2I electron microscopy 16.50 L 2-124 [» ]
4ADV electron microscopy 13.50 L 2-124 [» ]
4GAQ X-ray 3.30 L 1-124 [» ]
4GAS X-ray 3.30 L 1-124 [» ]
4GD1 X-ray 3.00 L 2-124 [» ]
4GD2 X-ray 3.00 L 2-124 [» ]
4KIY X-ray 2.90 L 1-124 [» ]
4KJ0 X-ray 2.90 L 1-124 [» ]
4KJ2 X-ray 2.90 L 1-124 [» ]
4KJ4 X-ray 2.90 L 1-124 [» ]
4KJ6 X-ray 2.90 L 1-124 [» ]
4KJ8 X-ray 2.90 L 1-124 [» ]
4KJA X-ray 2.90 L 1-124 [» ]
4KJC X-ray 2.90 L 1-124 [» ]
DisProti DP00145.
ProteinModelPortali P0A7S3.
SMRi P0A7S3. Positions 2-124.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 852156. 1 interaction.
DIPi DIP-35806N.
IntActi P0A7S3. 27 interactions.
STRINGi 511145.b3342.

Chemistry

ChEMBLi CHEMBL2363135.
DrugBanki DB00479. Amikacin.
DB00452. Framycetin.
DB00798. Gentamicin.
DB01172. Kanamycin.
DB00994. Neomycin.
DB00955. Netilmicin.
DB00919. Spectinomycin.
DB01082. Streptomycin.
DB00684. Tobramycin.

Proteomic databases

PaxDbi P0A7S3.
PRIDEi P0A7S3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76367 ; AAC76367 ; b3342 .
BAE77949 ; BAE77949 ; BAE77949 .
GeneIDi 12932620.
947845.
KEGGi ecj:Y75_p3834.
eco:b3342.
PATRICi 32122116. VBIEscCol129921_3435.

Organism-specific databases

EchoBASEi EB0904.
EcoGenei EG10911. rpsL.

Phylogenomic databases

eggNOGi COG0048.
HOGENOMi HOG000040063.
KOi K02950.
OMAi CYQRKGV.
OrthoDBi EOG61ZTNF.
PhylomeDBi P0A7S3.

Enzyme and pathway databases

BioCyci EcoCyc:EG10911-MONOMER.
ECOL316407:JW3304-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A7S3.
PROi P0A7S3.

Gene expression databases

Genevestigatori P0A7S3.

Family and domain databases

Gene3Di 2.40.50.140. 1 hit.
HAMAPi MF_00403_B. Ribosomal_S12_B.
InterProi IPR012340. NA-bd_OB-fold.
IPR006032. Ribosomal_S12/S23.
IPR005679. Ribosomal_S12_bac.
[Graphical view ]
PANTHERi PTHR11652. PTHR11652. 1 hit.
Pfami PF00164. Ribosom_S12_S23. 1 hit.
[Graphical view ]
PIRSFi PIRSF002133. Ribosomal_S12/S23. 1 hit.
PRINTSi PR01034. RIBOSOMALS12.
SUPFAMi SSF50249. SSF50249. 1 hit.
TIGRFAMsi TIGR00981. rpsL_bact. 1 hit.
PROSITEi PS00055. RIBOSOMAL_S12. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: 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. 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: July 9, 2014
This is version 108 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

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