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P17293

- RS12_THETH

UniProt

P17293 - RS12_THETH

Protein

30S ribosomal protein S12

Gene

rpsL

Organism
Thermus thermophilus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    With S4 and S5 plays an important role in translational accuracy.By similarity
    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

    GO - Molecular functioni

    1. rRNA binding Source: UniProtKB-HAMAP
    2. structural constituent of ribosome Source: InterPro
    3. tRNA binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. response to antibiotic Source: UniProtKB-KW
    2. translation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Biological processi

    Antibiotic resistance

    Keywords - Ligandi

    RNA-binding, rRNA-binding, tRNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    30S ribosomal protein S12
    Gene namesi
    Name:rpsL
    Synonyms:rps12
    OrganismiThermus thermophilus
    Taxonomic identifieri274 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

    Subcellular locationi

    GO - Cellular componenti

    1. small ribosomal subunit Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 13213130S ribosomal protein S12PRO_0000146342Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei89 – 8913-methylthioaspartic acidCurated

    Proteomic databases

    PRIDEiP17293.

    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

    Protein-protein interaction databases

    MINTiMINT-270023.
    STRINGi262724.TTC1333.

    Structurei

    Secondary structure

    1
    132
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 96
    Beta strandi24 – 263
    Beta strandi30 – 4011
    Beta strandi50 – 578
    Beta strandi62 – 665
    Beta strandi79 – 824
    Turni115 – 1184

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TWTmodel-O-[»]
    2OM7electron microscopy7.30E1-132[»]
    4BYBX-ray3.35L1-132[»]
    ProteinModelPortaliP17293.
    SMRiP17293. Positions 2-126.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP17293.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein S12P family.Curated

    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.

    P17293-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPTINQLVRK GREKVRKKSK VPALKGAPFR RGVCTVVRTV TPKKPNSALR    50
    KVAKVRLTSG YEVTAYIPGE GHNLQEHSVV LIRGGRVKDL PGVRYHIVRG 100
    VYDAAGVKDR KKSRSKYGTK KPKEAAKTAA KK 132
    Length:132
    Mass (Da):14,599
    Last modified:January 23, 2007 - v3
    Checksum:i9943D095FAD4D9BC
    GO

    Mass spectrometryi

    Molecular mass is 14516 Da from positions 2 - 132. Determined by MALDI. Strain IB-21.1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti42 – 421P → S in strain: Isolate HG18; streptomycin resistant.
    Natural varianti43 – 431K → R in strain: Isolate HG3; streptomycin resistant.
    Natural varianti86 – 861R → C in strain: Isolate HG14; streptomycin pseudo-dependent.
    Natural varianti86 – 861R → H in strain: Isolate HG31; streptomycin pseudo-dependent.
    Natural varianti88 – 881K → E in strain: Isolate HG19; streptomycin resistant.
    Natural varianti88 – 881K → R in strain: Isolate HG1; streptomycin resistant.
    Natural varianti91 – 911P → L in strain: Isolate HG11; streptomycin dependent.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF316617 Genomic DNA. Translation: AAG38586.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF316617 Genomic DNA. Translation: AAG38586.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TWT model - O - [» ]
    2OM7 electron microscopy 7.30 E 1-132 [» ]
    4BYB X-ray 3.35 L 1-132 [» ]
    ProteinModelPortali P17293.
    SMRi P17293. Positions 2-126.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-270023.
    STRINGi 262724.TTC1333.

    Proteomic databases

    PRIDEi P17293.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P17293.

    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. Cited for: PROTEIN SEQUENCE OF 2-8.
      Strain: VK1.
    2. "Streptomycin-resistant and streptomycin-dependent mutants of the extreme thermophile Thermus thermophilus."
      Gregory S.T., Cate J.H.D., Dahlberg A.E.
      J. Mol. Biol. 309:333-338(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-132, STREPTOMYCIN RESISTANT VARIANTS.
      Strain: ATCC 43815 / IB-21.
    3. "Extending ribosomal protein identifications to unsequenced bacterial strains using matrix-assisted laser desorption/ionization mass spectrometry."
      Suh M.-J., Hamburg D.M., Gregory S.T., Dahlberg A.E., Limbach P.A.
      Proteomics 5:4818-4831(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY.
      Strain: ATCC 43815 / IB-21.

    Entry informationi

    Entry nameiRS12_THETH
    AccessioniPrimary (citable) accession number: P17293
    Secondary accession number(s): Q9EYQ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 114 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Ribosomal proteins
      Ribosomal proteins families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3