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P0A7S3

- RS12_ECOLI

UniProt

P0A7S3 - RS12_ECOLI

Protein

30S ribosomal protein S12

Gene

rpsL

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    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. positive regulation of RNA splicing Source: EcoCyc
    3. response to antibiotic Source: UniProtKB-KW
    4. RNA folding Source: EcoCyc
    5. translation Source: EcoCyc

    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

    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 – 11Removed1 Publication
    Chaini2 – 12412330S ribosomal protein S12PRO_0000146219Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei89 – 8913-methylthioaspartic acid
    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.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 – 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A7S3.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein S12P family.Curated

    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

    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: October 1, 2014
    This is version 109 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