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P0A7V3

- RS3_ECOLI

UniProt

P0A7V3 - RS3_ECOLI

Protein

30S ribosomal protein S3

Gene

rpsC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation By similarity.By similarity
    Plays a role in mRNA unwinding by the ribosome, possibly by forming part of a processivity clamp.1 Publication

    GO - Molecular functioni

    1. DNA-(apurinic or apyrimidinic site) lyase activity Source: RefGenome
    2. mRNA binding Source: UniProtKB-HAMAP
    3. rRNA binding Source: UniProtKB-HAMAP
    4. structural constituent of ribosome Source: RefGenome

    GO - Biological processi

    1. cytoplasmic translation Source: RefGenome
    2. DNA catabolic process, endonucleolytic Source: GOC
    3. DNA repair Source: RefGenome
    4. regulation of apoptotic process Source: RefGenome

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    RNA-binding, rRNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10902-MONOMER.
    ECOL316407:JW3276-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    30S ribosomal protein S3
    Gene namesi
    Name:rpsC
    Ordered Locus Names:b3314, JW3276
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10902. rpsC.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosolic small ribosomal subunit Source: EcoCyc
    2. nucleus Source: RefGenome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi131 – 1355RRAMK → AAAMA: Decreases mRNA unwinding ability of the ribosome. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 23323230S ribosomal protein S3PRO_0000130113Add
    BLAST

    Proteomic databases

    PaxDbiP0A7V3.
    PRIDEiP0A7V3.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A7V3.

    Interactioni

    Subunit structurei

    Part of the 30S ribosomal subunit. Forms a tight complex with proteins S10 and S14 By similarity. With proteins S4 and S5 encircles the mRNA as it enters the ribosome, which may play a role in mRNA helicase processivity. Some nascent polypeptide chains are able to cross-link to this protein in situ.By similarity

    Protein-protein interaction databases

    BioGridi852126. 1 interaction.
    DIPiDIP-35807N.
    IntActiP0A7V3. 188 interactions.
    MINTiMINT-6478122.
    STRINGi511145.b3314.

    Structurei

    Secondary structure

    1
    233
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 113
    Turni12 – 154
    Beta strandi19 – 213
    Helixi26 – 4621
    Helixi47 – 493
    Beta strandi52 – 576
    Beta strandi61 – 644
    Beta strandi67 – 715
    Helixi73 – 775
    Turni78 – 814
    Helixi82 – 9514
    Beta strandi102 – 1054
    Helixi109 – 1113
    Helixi113 – 12513
    Helixi130 – 14314
    Beta strandi147 – 15610
    Helixi157 – 1593
    Beta strandi165 – 1717
    Beta strandi175 – 1773
    Beta strandi178 – 1803
    Beta strandi182 – 19110
    Beta strandi194 – 20310

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M5Gmodel-C2-207[»]
    1P6Gelectron microscopy12.30C2-233[»]
    1P87electron microscopy11.50C2-233[»]
    1VS5X-ray3.46C1-233[»]
    1VS7X-ray3.46C1-233[»]
    2AVYX-ray3.46C2-233[»]
    2AW7X-ray3.46C2-233[»]
    2GY9electron microscopy15.00C2-207[»]
    2GYBelectron microscopy15.00C2-207[»]
    2I2PX-ray3.22C2-233[»]
    2I2UX-ray3.22C2-233[»]
    2QALX-ray3.21C2-233[»]
    2QANX-ray3.21C2-233[»]
    2QB9X-ray3.54C2-233[»]
    2QBBX-ray3.54C2-233[»]
    2QBDX-ray3.30C2-233[»]
    2QBFX-ray3.30C2-233[»]
    2QBHX-ray4.00C2-233[»]
    2QBJX-ray4.00C2-233[»]
    2QOUX-ray3.93C2-233[»]
    2QOWX-ray3.93C2-233[»]
    2QOYX-ray3.50C2-233[»]
    2QP0X-ray3.50C2-233[»]
    2VHOX-ray3.74C2-233[»]
    2VHPX-ray3.74C2-233[»]
    2WWLelectron microscopy5.80C2-207[»]
    2YKRelectron microscopy9.80C2-207[»]
    2Z4KX-ray4.45C2-233[»]
    2Z4MX-ray4.45C2-233[»]
    3DF1X-ray3.50C2-232[»]
    3DF3X-ray3.50C2-232[»]
    3E1Aelectron microscopy-O1-233[»]
    3E1Celectron microscopy-O1-233[»]
    3FIHelectron microscopy6.70C2-207[»]
    3I1MX-ray3.19C1-233[»]
    3I1OX-ray3.19C1-233[»]
    3I1QX-ray3.81C1-233[»]
    3I1SX-ray3.81C1-233[»]
    3I1ZX-ray3.71C1-233[»]
    3I21X-ray3.71C1-233[»]
    3IZVelectron microscopy-G1-233[»]
    3IZWelectron microscopy-G1-233[»]
    3J00electron microscopy-C2-233[»]
    3J0Uelectron microscopy12.10F2-233[»]
    3J0Velectron microscopy14.70F2-233[»]
    3J0Xelectron microscopy13.50F2-233[»]
    3J0Zelectron microscopy11.50F2-233[»]
    3J10electron microscopy11.50F2-233[»]
    3J13electron microscopy13.10E2-233[»]
    3J18electron microscopy8.30C2-207[»]
    3J36electron microscopy9.80C2-233[»]
    3J4Velectron microscopy12.00C1-207[»]
    3J4Welectron microscopy12.00C1-207[»]
    3J4Yelectron microscopy17.00C1-207[»]
    3J4Zelectron microscopy20.00C1-207[»]
    3J53electron microscopy13.00C1-207[»]
    3J55electron microscopy15.00C1-207[»]
    3J57electron microscopy17.00C1-207[»]
    3J59electron microscopy12.00C1-207[»]
    3J5Belectron microscopy17.00C1-207[»]
    3J5Delectron microscopy17.00C1-207[»]
    3J5Felectron microscopy20.00C1-207[»]
    3J5Helectron microscopy15.00C1-207[»]
    3J5Jelectron microscopy9.00C1-207[»]
    3J5Nelectron microscopy6.80C1-233[»]
    3J5Telectron microscopy7.60C2-233[»]
    3J5Xelectron microscopy7.60C2-233[»]
    3KC4electron microscopy-C1-233[»]
    3OAQX-ray3.25C2-207[»]
    3OARX-ray3.25C2-207[»]
    3OFAX-ray3.19C2-207[»]
    3OFBX-ray3.19C2-207[»]
    3OFOX-ray3.10C2-207[»]
    3OFPX-ray3.10C2-207[»]
    3OFXX-ray3.29C2-207[»]
    3OFYX-ray3.29C2-207[»]
    3OR9X-ray3.30C1-233[»]
    3ORAX-ray3.30C1-233[»]
    3SFSX-ray3.20C1-233[»]
    3UOQX-ray3.70C1-233[»]
    4A2Ielectron microscopy16.50C2-207[»]
    4ADVelectron microscopy13.50C2-233[»]
    4GAQX-ray3.30C1-233[»]
    4GASX-ray3.30C1-233[»]
    4GD1X-ray3.00C2-207[»]
    4GD2X-ray3.00C2-207[»]
    4KIYX-ray2.90C1-233[»]
    4KJ0X-ray2.90C1-233[»]
    4KJ2X-ray2.90C1-233[»]
    4KJ4X-ray2.90C1-233[»]
    4KJ6X-ray2.90C1-233[»]
    4KJ8X-ray2.90C1-233[»]
    4KJAX-ray2.90C1-233[»]
    4KJCX-ray2.90C1-233[»]
    ProteinModelPortaliP0A7V3.
    SMRiP0A7V3. Positions 2-233.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A7V3.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini39 – 10769KH type-2Add
    BLAST

    Sequence similaritiesi

    Belongs to the ribosomal protein S3P family.Curated
    Contains 1 KH type-2 domain.Curated

    Phylogenomic databases

    eggNOGiCOG0092.
    HOGENOMiHOG000210610.
    KOiK02982.
    OMAiIARAEWY.
    OrthoDBiEOG6K13X3.
    PhylomeDBiP0A7V3.

    Family and domain databases

    Gene3Di3.30.1140.32. 1 hit.
    3.30.300.20. 1 hit.
    HAMAPiMF_01309_B. Ribosomal_S3_B.
    InterProiIPR004087. KH_dom.
    IPR015946. KH_dom-like_a/b.
    IPR004044. KH_dom_type_2.
    IPR009019. KH_prok-type.
    IPR005704. Ribosomal_S3_bac.
    IPR001351. Ribosomal_S3_C.
    IPR018280. Ribosomal_S3_CS.
    [Graphical view]
    PfamiPF07650. KH_2. 1 hit.
    PF00189. Ribosomal_S3_C. 1 hit.
    [Graphical view]
    SMARTiSM00322. KH. 1 hit.
    [Graphical view]
    SUPFAMiSSF54814. SSF54814. 1 hit.
    SSF54821. SSF54821. 1 hit.
    TIGRFAMsiTIGR01009. rpsC_bact. 1 hit.
    PROSITEiPS50823. KH_TYPE_2. 1 hit.
    PS00548. RIBOSOMAL_S3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0A7V3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGQKVHPNGI RLGIVKPWNS TWFANTKEFA DNLDSDFKVR QYLTKELAKA    50
    SVSRIVIERP AKSIRVTIHT ARPGIVIGKK GEDVEKLRKV VADIAGVPAQ 100
    INIAEVRKPE LDAKLVADSI TSQLERRVMF RRAMKRAVQN AMRLGAKGIK 150
    VEVSGRLGGA EIARTEWYRE GRVPLHTLRA DIDYNTSEAH TTYGVIGVKV 200
    WIFKGEILGG MAAVEQPEKP AAQPKKQQRK GRK 233
    Length:233
    Mass (Da):25,983
    Last modified:January 23, 2007 - v2
    Checksum:i6D0131A285B7AAB3
    GO

    Mass spectrometryi

    Molecular mass is 25851.9 Da from positions 2 - 233. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02613 Genomic DNA. Translation: CAA26466.1.
    U18997 Genomic DNA. Translation: AAA58111.1.
    U00096 Genomic DNA. Translation: AAC76339.1.
    AP009048 Genomic DNA. Translation: BAE77977.1.
    PIRiH23129. R3EC3.
    RefSeqiNP_417773.1. NC_000913.3.
    YP_492118.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76339; AAC76339; b3314.
    BAE77977; BAE77977; BAE77977.
    GeneIDi12932292.
    947814.
    KEGGiecj:Y75_p3862.
    eco:b3314.
    PATRICi32122060. VBIEscCol129921_3407.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02613 Genomic DNA. Translation: CAA26466.1 .
    U18997 Genomic DNA. Translation: AAA58111.1 .
    U00096 Genomic DNA. Translation: AAC76339.1 .
    AP009048 Genomic DNA. Translation: BAE77977.1 .
    PIRi H23129. R3EC3.
    RefSeqi NP_417773.1. NC_000913.3.
    YP_492118.1. 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 - C 2-207 [» ]
    1P6G electron microscopy 12.30 C 2-233 [» ]
    1P87 electron microscopy 11.50 C 2-233 [» ]
    1VS5 X-ray 3.46 C 1-233 [» ]
    1VS7 X-ray 3.46 C 1-233 [» ]
    2AVY X-ray 3.46 C 2-233 [» ]
    2AW7 X-ray 3.46 C 2-233 [» ]
    2GY9 electron microscopy 15.00 C 2-207 [» ]
    2GYB electron microscopy 15.00 C 2-207 [» ]
    2I2P X-ray 3.22 C 2-233 [» ]
    2I2U X-ray 3.22 C 2-233 [» ]
    2QAL X-ray 3.21 C 2-233 [» ]
    2QAN X-ray 3.21 C 2-233 [» ]
    2QB9 X-ray 3.54 C 2-233 [» ]
    2QBB X-ray 3.54 C 2-233 [» ]
    2QBD X-ray 3.30 C 2-233 [» ]
    2QBF X-ray 3.30 C 2-233 [» ]
    2QBH X-ray 4.00 C 2-233 [» ]
    2QBJ X-ray 4.00 C 2-233 [» ]
    2QOU X-ray 3.93 C 2-233 [» ]
    2QOW X-ray 3.93 C 2-233 [» ]
    2QOY X-ray 3.50 C 2-233 [» ]
    2QP0 X-ray 3.50 C 2-233 [» ]
    2VHO X-ray 3.74 C 2-233 [» ]
    2VHP X-ray 3.74 C 2-233 [» ]
    2WWL electron microscopy 5.80 C 2-207 [» ]
    2YKR electron microscopy 9.80 C 2-207 [» ]
    2Z4K X-ray 4.45 C 2-233 [» ]
    2Z4M X-ray 4.45 C 2-233 [» ]
    3DF1 X-ray 3.50 C 2-232 [» ]
    3DF3 X-ray 3.50 C 2-232 [» ]
    3E1A electron microscopy - O 1-233 [» ]
    3E1C electron microscopy - O 1-233 [» ]
    3FIH electron microscopy 6.70 C 2-207 [» ]
    3I1M X-ray 3.19 C 1-233 [» ]
    3I1O X-ray 3.19 C 1-233 [» ]
    3I1Q X-ray 3.81 C 1-233 [» ]
    3I1S X-ray 3.81 C 1-233 [» ]
    3I1Z X-ray 3.71 C 1-233 [» ]
    3I21 X-ray 3.71 C 1-233 [» ]
    3IZV electron microscopy - G 1-233 [» ]
    3IZW electron microscopy - G 1-233 [» ]
    3J00 electron microscopy - C 2-233 [» ]
    3J0U electron microscopy 12.10 F 2-233 [» ]
    3J0V electron microscopy 14.70 F 2-233 [» ]
    3J0X electron microscopy 13.50 F 2-233 [» ]
    3J0Z electron microscopy 11.50 F 2-233 [» ]
    3J10 electron microscopy 11.50 F 2-233 [» ]
    3J13 electron microscopy 13.10 E 2-233 [» ]
    3J18 electron microscopy 8.30 C 2-207 [» ]
    3J36 electron microscopy 9.80 C 2-233 [» ]
    3J4V electron microscopy 12.00 C 1-207 [» ]
    3J4W electron microscopy 12.00 C 1-207 [» ]
    3J4Y electron microscopy 17.00 C 1-207 [» ]
    3J4Z electron microscopy 20.00 C 1-207 [» ]
    3J53 electron microscopy 13.00 C 1-207 [» ]
    3J55 electron microscopy 15.00 C 1-207 [» ]
    3J57 electron microscopy 17.00 C 1-207 [» ]
    3J59 electron microscopy 12.00 C 1-207 [» ]
    3J5B electron microscopy 17.00 C 1-207 [» ]
    3J5D electron microscopy 17.00 C 1-207 [» ]
    3J5F electron microscopy 20.00 C 1-207 [» ]
    3J5H electron microscopy 15.00 C 1-207 [» ]
    3J5J electron microscopy 9.00 C 1-207 [» ]
    3J5N electron microscopy 6.80 C 1-233 [» ]
    3J5T electron microscopy 7.60 C 2-233 [» ]
    3J5X electron microscopy 7.60 C 2-233 [» ]
    3KC4 electron microscopy - C 1-233 [» ]
    3OAQ X-ray 3.25 C 2-207 [» ]
    3OAR X-ray 3.25 C 2-207 [» ]
    3OFA X-ray 3.19 C 2-207 [» ]
    3OFB X-ray 3.19 C 2-207 [» ]
    3OFO X-ray 3.10 C 2-207 [» ]
    3OFP X-ray 3.10 C 2-207 [» ]
    3OFX X-ray 3.29 C 2-207 [» ]
    3OFY X-ray 3.29 C 2-207 [» ]
    3OR9 X-ray 3.30 C 1-233 [» ]
    3ORA X-ray 3.30 C 1-233 [» ]
    3SFS X-ray 3.20 C 1-233 [» ]
    3UOQ X-ray 3.70 C 1-233 [» ]
    4A2I electron microscopy 16.50 C 2-207 [» ]
    4ADV electron microscopy 13.50 C 2-233 [» ]
    4GAQ X-ray 3.30 C 1-233 [» ]
    4GAS X-ray 3.30 C 1-233 [» ]
    4GD1 X-ray 3.00 C 2-207 [» ]
    4GD2 X-ray 3.00 C 2-207 [» ]
    4KIY X-ray 2.90 C 1-233 [» ]
    4KJ0 X-ray 2.90 C 1-233 [» ]
    4KJ2 X-ray 2.90 C 1-233 [» ]
    4KJ4 X-ray 2.90 C 1-233 [» ]
    4KJ6 X-ray 2.90 C 1-233 [» ]
    4KJ8 X-ray 2.90 C 1-233 [» ]
    4KJA X-ray 2.90 C 1-233 [» ]
    4KJC X-ray 2.90 C 1-233 [» ]
    ProteinModelPortali P0A7V3.
    SMRi P0A7V3. Positions 2-233.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 852126. 1 interaction.
    DIPi DIP-35807N.
    IntActi P0A7V3. 188 interactions.
    MINTi MINT-6478122.
    STRINGi 511145.b3314.

    Chemistry

    ChEMBLi CHEMBL2363135.

    Proteomic databases

    PaxDbi P0A7V3.
    PRIDEi P0A7V3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76339 ; AAC76339 ; b3314 .
    BAE77977 ; BAE77977 ; BAE77977 .
    GeneIDi 12932292.
    947814.
    KEGGi ecj:Y75_p3862.
    eco:b3314.
    PATRICi 32122060. VBIEscCol129921_3407.

    Organism-specific databases

    EchoBASEi EB0895.
    EcoGenei EG10902. rpsC.

    Phylogenomic databases

    eggNOGi COG0092.
    HOGENOMi HOG000210610.
    KOi K02982.
    OMAi IARAEWY.
    OrthoDBi EOG6K13X3.
    PhylomeDBi P0A7V3.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10902-MONOMER.
    ECOL316407:JW3276-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A7V3.
    PROi P0A7V3.

    Gene expression databases

    Genevestigatori P0A7V3.

    Family and domain databases

    Gene3Di 3.30.1140.32. 1 hit.
    3.30.300.20. 1 hit.
    HAMAPi MF_01309_B. Ribosomal_S3_B.
    InterProi IPR004087. KH_dom.
    IPR015946. KH_dom-like_a/b.
    IPR004044. KH_dom_type_2.
    IPR009019. KH_prok-type.
    IPR005704. Ribosomal_S3_bac.
    IPR001351. Ribosomal_S3_C.
    IPR018280. Ribosomal_S3_CS.
    [Graphical view ]
    Pfami PF07650. KH_2. 1 hit.
    PF00189. Ribosomal_S3_C. 1 hit.
    [Graphical view ]
    SMARTi SM00322. KH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54814. SSF54814. 1 hit.
    SSF54821. SSF54821. 1 hit.
    TIGRFAMsi TIGR01009. rpsC_bact. 1 hit.
    PROSITEi PS50823. KH_TYPE_2. 1 hit.
    PS00548. RIBOSOMAL_S3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure of the Escherichia coli S10 ribosomal protein operon."
      Zurawski G., Zurawski S.M.
      Nucleic Acids Res. 13:4521-4526(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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.
    4. "The primary structure of protein S3 from the small ribosomal subunit of Escherichia coli."
      Brauer D., Roming R.
      FEBS Lett. 106:352-357(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-233.
      Strain: K.
    5. "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 39-49 AND 87-108, CROSS-LINKING TO RRNA.
      Strain: MRE-600.
    6. "Flexibility of the nascent polypeptide chain within the ribosome --contacts from the peptide N-terminus to a specific region of the 30S subunit."
      Choi K.M., Atkins J.F., Gesteland R.F., Brimacombe R.
      Eur. J. Biochem. 255:409-413(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CROSS-LINKING TO NASCENT POLYPEPTIDE CHAINS.
    7. "mRNA helicase activity of the ribosome."
      Takyar S., Hickerson R.P., Noller H.F.
      Cell 120:49-58(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN MRNA HELICASE ACTIVITY, MUTAGENESIS.
      Strain: MRE-600.
    8. "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.
    9. "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.
    10. "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.
    11. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
      Strain: MRE-600.

    Entry informationi

    Entry nameiRS3_ECOLI
    AccessioniPrimary (citable) accession number: P0A7V3
    Secondary accession number(s): P02352, Q2M6X9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 103 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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