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P02357

- RS5_GEOSE

UniProt

P02357 - RS5_GEOSE

Protein

30S ribosomal protein S5

Gene

rpsE

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    With S4 and S12 plays an important role in translational accuracy.By similarity
    Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body.By similarity

    GO - Molecular functioni

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    30S ribosomal protein S5
    Short name:
    BS5
    Alternative name(s):
    BS6
    Gene namesi
    Name:rpsE
    OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
    Taxonomic identifieri1422 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

    Subcellular locationi

    GO - Cellular componenti

    1. small ribosomal subunit Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 16616630S ribosomal protein S5PRO_0000131469Add
    BLAST

    Interactioni

    Subunit structurei

    Part of the 30S ribosomal subunit. Contacts proteins S4 and S8 By similarity.By similarity

    Protein-protein interaction databases

    MINTiMINT-112114.

    Structurei

    Secondary structure

    1
    166
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 83
    Beta strandi12 – 198
    Beta strandi21 – 244
    Beta strandi33 – 408
    Beta strandi42 – 5514
    Helixi56 – 6712
    Beta strandi85 – 895
    Beta strandi92 – 987
    Beta strandi105 – 1073
    Helixi109 – 11810
    Beta strandi122 – 1276
    Helixi133 – 14614

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DV4X-ray4.50E4-148[»]
    1PKPX-ray2.80A1-150[»]
    ProteinModelPortaliP02357.
    SMRiP02357. Positions 4-148.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02357.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 7464S5 DRBMAdd
    BLAST

    Domaini

    The N-terminal domain interacts with the head of the 30S subunit; the C-terminal domain interacts with the body and contacts protein S4. The interaction surface between S4 and S5 is involved in control of translational fidelity.

    Sequence similaritiesi

    Belongs to the ribosomal protein S5P family.Curated
    Contains 1 S5 DRBM domain.Curated

    Family and domain databases

    Gene3Di3.30.160.20. 1 hit.
    3.30.230.10. 1 hit.
    HAMAPiMF_01307_B. Ribosomal_S5_B.
    InterProiIPR014720. dsRNA-bd_dom.
    IPR000851. Ribosomal_S5.
    IPR005712. Ribosomal_S5_bac-type.
    IPR005324. Ribosomal_S5_C.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR013810. Ribosomal_S5_N.
    IPR018192. Ribosomal_S5_N_CS.
    [Graphical view]
    PANTHERiPTHR13718. PTHR13718. 1 hit.
    PfamiPF00333. Ribosomal_S5. 1 hit.
    PF03719. Ribosomal_S5_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF54211. SSF54211. 1 hit.
    TIGRFAMsiTIGR01021. rpsE_bact. 1 hit.
    PROSITEiPS00585. RIBOSOMAL_S5. 1 hit.
    PS50881. S5_DSRBD. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P02357-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRRINPNKLE LEERVVAVNR VAKVVKGGRR LRFSALVVVG DKNGHVGFGT    50
    GKAQEVPEAI RKAIEDAKKN LIEVPIVGTT IPHEVIGHFG AGEIILKPAS 100
    EGTGVIAGGP ARAVLELAGI SDILSKSIGS NTPINMVRAT FDGLKQLKRA 150
    EDVAKLRGKT VEELLG 166
    Length:166
    Mass (Da):17,628
    Last modified:July 21, 1986 - v1
    Checksum:i774E82A2ED1D8EC5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57621 Genomic DNA. Translation: AAA22699.1.
    PIRiA02708. R3BS5F.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57621 Genomic DNA. Translation: AAA22699.1 .
    PIRi A02708. R3BS5F.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DV4 X-ray 4.50 E 4-148 [» ]
    1PKP X-ray 2.80 A 1-150 [» ]
    ProteinModelPortali P02357.
    SMRi P02357. Positions 4-148.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-112114.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P02357.

    Family and domain databases

    Gene3Di 3.30.160.20. 1 hit.
    3.30.230.10. 1 hit.
    HAMAPi MF_01307_B. Ribosomal_S5_B.
    InterProi IPR014720. dsRNA-bd_dom.
    IPR000851. Ribosomal_S5.
    IPR005712. Ribosomal_S5_bac-type.
    IPR005324. Ribosomal_S5_C.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR013810. Ribosomal_S5_N.
    IPR018192. Ribosomal_S5_N_CS.
    [Graphical view ]
    PANTHERi PTHR13718. PTHR13718. 1 hit.
    Pfami PF00333. Ribosomal_S5. 1 hit.
    PF03719. Ribosomal_S5_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54211. SSF54211. 1 hit.
    TIGRFAMsi TIGR01021. rpsE_bact. 1 hit.
    PROSITEi PS00585. RIBOSOMAL_S5. 1 hit.
    PS50881. S5_DSRBD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Proteins of the Bacillus stearothermophilus ribosome. The amino acid sequences of proteins S5 and L30."
      Kimura M.
      J. Biol. Chem. 259:1051-1055(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
      Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924.
    2. "Cloning, sequencing, and overexpression of genes for ribosomal proteins from Bacillus stearothermophilus."
      Ramakrishnan V., Gerchman S.E.
      J. Biol. Chem. 266:880-885(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Procaryotic ribosomal proteins: N-terminal sequence homologies and structural correspondence of 30 S ribosomal proteins from Escherichia coli and Bacillus stearothermophilus."
      Yaguchi M., Matheson A.T., Visentin L.P.
      FEBS Lett. 46:296-300(1974) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-15.
      Strain: DSM 13240 / CIP 106956 / 10.
    4. "Isolation and characterization of Bacillus stearothermophilus 30S and 50S ribosomal protein mutations."
      Schnier J., Gewitz H.S., Behrens S.E., Lee A., Ginther C., Leighton T.
      J. Bacteriol. 172:7306-7309(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: ISOLATION OF STREPTOMYCIN INDEPENDENT STRAINS.
      Strain: 799.
    5. "The structure of ribosomal protein S5 reveals sites of interaction with 16S rRNA."
      Ramakrishnan V., White S.W.
      Nature 358:768-771(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
    6. "Ribosomal proteins S5 and L6: high-resolution crystal structures and roles in protein synthesis and antibiotic resistance."
      Davies C., Bussiere D.E., Golden B.L., Porter S.J., Ramakrishnan V., White S.W.
      J. Mol. Biol. 279:873-888(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

    Entry informationi

    Entry nameiRS5_GEOSE
    AccessioniPrimary (citable) accession number: P02357
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 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