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P0A7X3

- RS9_ECOLI

UniProt

P0A7X3 - RS9_ECOLI

Protein

30S ribosomal protein S9

Gene

rpsI

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    The C-terminal tail plays a role in the affinity of the 30S P site for different tRNAs. Mutations that decrease this affinity are suppressed in the 70S ribosome.1 Publication

    GO - Molecular functioni

    1. structural constituent of ribosome Source: InterPro
    2. tRNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. translation Source: InterPro

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    RNA-binding, tRNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10908-MONOMER.
    ECOL316407:JW3199-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    30S ribosomal protein S9
    Gene namesi
    Name:rpsI
    Ordered Locus Names:b3230, JW3199
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10908. rpsI.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosolic small ribosomal subunit Source: EcoCyc

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi105 – 13026Missing: Cold sensitive for growth at 30 degrees Celsius. 350-fold reduced affinity of the 30S subunit P site for certain tRNAs in vitro. 1 PublicationAdd
    BLAST
    Mutagenesisi128 – 1303Missing: Very cold sensitive for growth at 30 degrees Celsius. Almost no P site binding of certain tRNAs in vitro. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 13012930S ribosomal protein S9PRO_0000111354Add
    BLAST

    Proteomic databases

    PaxDbiP0A7X3.
    PRIDEiP0A7X3.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A7X3.

    Interactioni

    Subunit structurei

    Part of the 30S ribosomal subunit. Cross-links to the P site tRNA and weakly to the A site tRNA.

    Protein-protein interaction databases

    DIPiDIP-35799N.
    IntActiP0A7X3. 148 interactions.
    MINTiMINT-1290939.
    STRINGi511145.b3230.

    Structurei

    Secondary structure

    1
    130
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 83
    Beta strandi11 – 144
    Beta strandi17 – 248
    Beta strandi28 – 303
    Helixi35 – 384
    Turni39 – 413
    Turni43 – 508
    Helixi51 – 544
    Beta strandi60 – 678
    Beta strandi68 – 703
    Helixi72 – 8615
    Helixi87 – 893
    Turni91 – 933
    Helixi94 – 1007
    Turni102 – 1043
    Beta strandi118 – 1203

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M5Gmodel-I4-130[»]
    1P6Gelectron microscopy12.30I2-130[»]
    1P87electron microscopy11.50I2-130[»]
    1VS5X-ray3.46I1-130[»]
    1VS7X-ray3.46I1-130[»]
    2AVYX-ray3.46I2-130[»]
    2AW7X-ray3.46I2-130[»]
    2GY9electron microscopy15.00I5-130[»]
    2GYBelectron microscopy15.00I5-130[»]
    2I2PX-ray3.22I2-130[»]
    2I2UX-ray3.22I2-130[»]
    2QALX-ray3.21I2-130[»]
    2QANX-ray3.21I2-130[»]
    2QB9X-ray3.54I2-130[»]
    2QBBX-ray3.54I2-130[»]
    2QBDX-ray3.30I2-130[»]
    2QBFX-ray3.30I2-130[»]
    2QBHX-ray4.00I2-130[»]
    2QBJX-ray4.00I2-130[»]
    2QOUX-ray3.93I2-130[»]
    2QOWX-ray3.93I2-130[»]
    2QOYX-ray3.50I2-130[»]
    2QP0X-ray3.50I2-130[»]
    2VHOX-ray3.74I2-130[»]
    2VHPX-ray3.74I2-130[»]
    2WWLelectron microscopy5.80I4-130[»]
    2YKRelectron microscopy9.80I4-130[»]
    2Z4KX-ray4.45I2-130[»]
    2Z4MX-ray4.45I2-130[»]
    3DF1X-ray3.50I2-129[»]
    3DF3X-ray3.50I2-129[»]
    3E1Aelectron microscopy-W1-130[»]
    3E1Celectron microscopy-W1-130[»]
    3FIHelectron microscopy6.70I4-130[»]
    3I1MX-ray3.19I1-130[»]
    3I1OX-ray3.19I1-130[»]
    3I1QX-ray3.81I1-130[»]
    3I1SX-ray3.81I1-130[»]
    3I1ZX-ray3.71I1-130[»]
    3I21X-ray3.71I1-130[»]
    3IZVelectron microscopy-M1-130[»]
    3IZWelectron microscopy-M1-130[»]
    3J00electron microscopy-I2-130[»]
    3J0Uelectron microscopy12.10L2-130[»]
    3J0Velectron microscopy14.70L2-130[»]
    3J0Xelectron microscopy13.50L2-130[»]
    3J0Zelectron microscopy11.50L2-130[»]
    3J10electron microscopy11.50L2-130[»]
    3J13electron microscopy13.10K2-130[»]
    3J18electron microscopy8.30I4-130[»]
    3J36electron microscopy9.80I2-130[»]
    3J4Velectron microscopy12.00I4-130[»]
    3J4Welectron microscopy12.00I4-130[»]
    3J4Yelectron microscopy17.00I4-130[»]
    3J4Zelectron microscopy20.00I4-130[»]
    3J53electron microscopy13.00I4-130[»]
    3J55electron microscopy15.00I4-130[»]
    3J57electron microscopy17.00I4-130[»]
    3J59electron microscopy12.00I4-130[»]
    3J5Belectron microscopy17.00I4-130[»]
    3J5Delectron microscopy17.00I4-130[»]
    3J5Felectron microscopy20.00I4-130[»]
    3J5Helectron microscopy15.00I4-130[»]
    3J5Jelectron microscopy9.00I4-130[»]
    3J5Nelectron microscopy6.80I1-130[»]
    3J5Telectron microscopy7.60I2-130[»]
    3J5Xelectron microscopy7.60I2-130[»]
    3KC4electron microscopy-I1-130[»]
    3OAQX-ray3.25I4-130[»]
    3OARX-ray3.25I4-130[»]
    3OFAX-ray3.19I4-130[»]
    3OFBX-ray3.19I4-130[»]
    3OFOX-ray3.10I4-130[»]
    3OFPX-ray3.10I4-130[»]
    3OFXX-ray3.29I4-130[»]
    3OFYX-ray3.29I4-130[»]
    3OR9X-ray3.30I1-130[»]
    3ORAX-ray3.30I1-130[»]
    3SFSX-ray3.20I1-130[»]
    3UOQX-ray3.70I1-130[»]
    4A2Ielectron microscopy16.50I4-130[»]
    4ADVelectron microscopy13.50I2-130[»]
    4GAQX-ray3.30I1-130[»]
    4GASX-ray3.30I1-130[»]
    4GD1X-ray3.00I4-130[»]
    4GD2X-ray3.00I4-130[»]
    4KIYX-ray2.90I1-130[»]
    4KJ0X-ray2.90I1-130[»]
    4KJ2X-ray2.90I1-130[»]
    4KJ4X-ray2.90I1-130[»]
    4KJ6X-ray2.90I1-130[»]
    4KJ8X-ray2.90I1-130[»]
    4KJAX-ray2.90I1-130[»]
    4KJCX-ray2.90I1-130[»]
    ProteinModelPortaliP0A7X3.
    SMRiP0A7X3. Positions 4-130.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A7X3.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein S9P family.Curated

    Phylogenomic databases

    eggNOGiCOG0103.
    HOGENOMiHOG000019802.
    KOiK02996.
    OMAiLMDYDET.
    OrthoDBiEOG6MWNH0.
    PhylomeDBiP0A7X3.

    Family and domain databases

    Gene3Di3.30.230.10. 1 hit.
    HAMAPiMF_00532_B. Ribosomal_S9_B.
    InterProiIPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR000754. Ribosomal_S9.
    IPR023035. Ribosomal_S9_bac/plastid.
    IPR020574. Ribosomal_S9_CS.
    [Graphical view]
    PANTHERiPTHR21569. PTHR21569. 1 hit.
    PfamiPF00380. Ribosomal_S9. 1 hit.
    [Graphical view]
    SUPFAMiSSF54211. SSF54211. 1 hit.
    PROSITEiPS00360. RIBOSOMAL_S9. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0A7X3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAENQYYGTG RRKSSAARVF IKPGNGKIVI NQRSLEQYFG RETARMVVRQ    50
    PLELVDMVEK LDLYITVKGG GISGQAGAIR HGITRALMEY DESLRSELRK 100
    AGFVTRDARQ VERKKVGLRK ARRRPQFSKR 130
    Length:130
    Mass (Da):14,856
    Last modified:January 23, 2007 - v2
    Checksum:i757D599168812806
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti56 – 561D → N AA sequence (PubMed:1091515)Curated
    Sequence conflicti124 – 1241Missing AA sequence (PubMed:1091515)Curated
    Sequence conflicti126 – 1261Q → E AA sequence (PubMed:1091515)Curated

    Mass spectrometryi

    Molecular mass is 14723.3 Da from positions 2 - 130. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02130 Genomic DNA. Translation: CAA26042.1.
    U18997 Genomic DNA. Translation: AAA58032.1.
    U00096 Genomic DNA. Translation: AAC76262.1.
    AP009048 Genomic DNA. Translation: BAE77273.1.
    PIRiH65114. R3EC9.
    RefSeqiNP_417697.1. NC_000913.3.
    YP_491414.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76262; AAC76262; b3230.
    BAE77273; BAE77273; BAE77273.
    GeneIDi12933452.
    949000.
    KEGGiecj:Y75_p3150.
    eco:b3230.
    PATRICi32121886. VBIEscCol129921_3327.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02130 Genomic DNA. Translation: CAA26042.1 .
    U18997 Genomic DNA. Translation: AAA58032.1 .
    U00096 Genomic DNA. Translation: AAC76262.1 .
    AP009048 Genomic DNA. Translation: BAE77273.1 .
    PIRi H65114. R3EC9.
    RefSeqi NP_417697.1. NC_000913.3.
    YP_491414.1. 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 - I 4-130 [» ]
    1P6G electron microscopy 12.30 I 2-130 [» ]
    1P87 electron microscopy 11.50 I 2-130 [» ]
    1VS5 X-ray 3.46 I 1-130 [» ]
    1VS7 X-ray 3.46 I 1-130 [» ]
    2AVY X-ray 3.46 I 2-130 [» ]
    2AW7 X-ray 3.46 I 2-130 [» ]
    2GY9 electron microscopy 15.00 I 5-130 [» ]
    2GYB electron microscopy 15.00 I 5-130 [» ]
    2I2P X-ray 3.22 I 2-130 [» ]
    2I2U X-ray 3.22 I 2-130 [» ]
    2QAL X-ray 3.21 I 2-130 [» ]
    2QAN X-ray 3.21 I 2-130 [» ]
    2QB9 X-ray 3.54 I 2-130 [» ]
    2QBB X-ray 3.54 I 2-130 [» ]
    2QBD X-ray 3.30 I 2-130 [» ]
    2QBF X-ray 3.30 I 2-130 [» ]
    2QBH X-ray 4.00 I 2-130 [» ]
    2QBJ X-ray 4.00 I 2-130 [» ]
    2QOU X-ray 3.93 I 2-130 [» ]
    2QOW X-ray 3.93 I 2-130 [» ]
    2QOY X-ray 3.50 I 2-130 [» ]
    2QP0 X-ray 3.50 I 2-130 [» ]
    2VHO X-ray 3.74 I 2-130 [» ]
    2VHP X-ray 3.74 I 2-130 [» ]
    2WWL electron microscopy 5.80 I 4-130 [» ]
    2YKR electron microscopy 9.80 I 4-130 [» ]
    2Z4K X-ray 4.45 I 2-130 [» ]
    2Z4M X-ray 4.45 I 2-130 [» ]
    3DF1 X-ray 3.50 I 2-129 [» ]
    3DF3 X-ray 3.50 I 2-129 [» ]
    3E1A electron microscopy - W 1-130 [» ]
    3E1C electron microscopy - W 1-130 [» ]
    3FIH electron microscopy 6.70 I 4-130 [» ]
    3I1M X-ray 3.19 I 1-130 [» ]
    3I1O X-ray 3.19 I 1-130 [» ]
    3I1Q X-ray 3.81 I 1-130 [» ]
    3I1S X-ray 3.81 I 1-130 [» ]
    3I1Z X-ray 3.71 I 1-130 [» ]
    3I21 X-ray 3.71 I 1-130 [» ]
    3IZV electron microscopy - M 1-130 [» ]
    3IZW electron microscopy - M 1-130 [» ]
    3J00 electron microscopy - I 2-130 [» ]
    3J0U electron microscopy 12.10 L 2-130 [» ]
    3J0V electron microscopy 14.70 L 2-130 [» ]
    3J0X electron microscopy 13.50 L 2-130 [» ]
    3J0Z electron microscopy 11.50 L 2-130 [» ]
    3J10 electron microscopy 11.50 L 2-130 [» ]
    3J13 electron microscopy 13.10 K 2-130 [» ]
    3J18 electron microscopy 8.30 I 4-130 [» ]
    3J36 electron microscopy 9.80 I 2-130 [» ]
    3J4V electron microscopy 12.00 I 4-130 [» ]
    3J4W electron microscopy 12.00 I 4-130 [» ]
    3J4Y electron microscopy 17.00 I 4-130 [» ]
    3J4Z electron microscopy 20.00 I 4-130 [» ]
    3J53 electron microscopy 13.00 I 4-130 [» ]
    3J55 electron microscopy 15.00 I 4-130 [» ]
    3J57 electron microscopy 17.00 I 4-130 [» ]
    3J59 electron microscopy 12.00 I 4-130 [» ]
    3J5B electron microscopy 17.00 I 4-130 [» ]
    3J5D electron microscopy 17.00 I 4-130 [» ]
    3J5F electron microscopy 20.00 I 4-130 [» ]
    3J5H electron microscopy 15.00 I 4-130 [» ]
    3J5J electron microscopy 9.00 I 4-130 [» ]
    3J5N electron microscopy 6.80 I 1-130 [» ]
    3J5T electron microscopy 7.60 I 2-130 [» ]
    3J5X electron microscopy 7.60 I 2-130 [» ]
    3KC4 electron microscopy - I 1-130 [» ]
    3OAQ X-ray 3.25 I 4-130 [» ]
    3OAR X-ray 3.25 I 4-130 [» ]
    3OFA X-ray 3.19 I 4-130 [» ]
    3OFB X-ray 3.19 I 4-130 [» ]
    3OFO X-ray 3.10 I 4-130 [» ]
    3OFP X-ray 3.10 I 4-130 [» ]
    3OFX X-ray 3.29 I 4-130 [» ]
    3OFY X-ray 3.29 I 4-130 [» ]
    3OR9 X-ray 3.30 I 1-130 [» ]
    3ORA X-ray 3.30 I 1-130 [» ]
    3SFS X-ray 3.20 I 1-130 [» ]
    3UOQ X-ray 3.70 I 1-130 [» ]
    4A2I electron microscopy 16.50 I 4-130 [» ]
    4ADV electron microscopy 13.50 I 2-130 [» ]
    4GAQ X-ray 3.30 I 1-130 [» ]
    4GAS X-ray 3.30 I 1-130 [» ]
    4GD1 X-ray 3.00 I 4-130 [» ]
    4GD2 X-ray 3.00 I 4-130 [» ]
    4KIY X-ray 2.90 I 1-130 [» ]
    4KJ0 X-ray 2.90 I 1-130 [» ]
    4KJ2 X-ray 2.90 I 1-130 [» ]
    4KJ4 X-ray 2.90 I 1-130 [» ]
    4KJ6 X-ray 2.90 I 1-130 [» ]
    4KJ8 X-ray 2.90 I 1-130 [» ]
    4KJA X-ray 2.90 I 1-130 [» ]
    4KJC X-ray 2.90 I 1-130 [» ]
    ProteinModelPortali P0A7X3.
    SMRi P0A7X3. Positions 4-130.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35799N.
    IntActi P0A7X3. 148 interactions.
    MINTi MINT-1290939.
    STRINGi 511145.b3230.

    Chemistry

    ChEMBLi CHEMBL2363135.
    DrugBanki DB00453. Clomocycline.
    DB00618. Demeclocycline.
    DB00254. Doxycycline.
    DB00256. Lymecycline.
    DB01017. Minocycline.
    DB00595. Oxytetracycline.
    DB00759. Tetracycline.
    DB00560. Tigecycline.

    Proteomic databases

    PaxDbi P0A7X3.
    PRIDEi P0A7X3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76262 ; AAC76262 ; b3230 .
    BAE77273 ; BAE77273 ; BAE77273 .
    GeneIDi 12933452.
    949000.
    KEGGi ecj:Y75_p3150.
    eco:b3230.
    PATRICi 32121886. VBIEscCol129921_3327.

    Organism-specific databases

    EchoBASEi EB0901.
    EcoGenei EG10908. rpsI.

    Phylogenomic databases

    eggNOGi COG0103.
    HOGENOMi HOG000019802.
    KOi K02996.
    OMAi LMDYDET.
    OrthoDBi EOG6MWNH0.
    PhylomeDBi P0A7X3.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10908-MONOMER.
    ECOL316407:JW3199-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A7X3.
    PROi P0A7X3.

    Gene expression databases

    Genevestigatori P0A7X3.

    Family and domain databases

    Gene3Di 3.30.230.10. 1 hit.
    HAMAPi MF_00532_B. Ribosomal_S9_B.
    InterProi IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR000754. Ribosomal_S9.
    IPR023035. Ribosomal_S9_bac/plastid.
    IPR020574. Ribosomal_S9_CS.
    [Graphical view ]
    PANTHERi PTHR21569. PTHR21569. 1 hit.
    Pfami PF00380. Ribosomal_S9. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54211. SSF54211. 1 hit.
    PROSITEi PS00360. RIBOSOMAL_S9. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and nucleotide sequencing of the genes for ribosomal proteins S9 (rpsI) and L13 (rplM) of Escherichia coli."
      Isono S., Thamm S., Kitakawa M., Isono K.
      Mol. Gen. Genet. 198:279-282(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 S9 from the 30S subunit of Escherichia coli ribosomes."
      Chen R., Wittmann-Liebold B.
      FEBS Lett. 52:139-140(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-130.
      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 121-130, CROSS-LINKING TO RRNA.
      Strain: MRE-600.
    6. "Requirement of proteins S5 and S9 from 30S subunits for the ribosome-dependent GTPase activity of elongation factor G."
      Marsh R.C., Parmeggiani A.
      Proc. Natl. Acad. Sci. U.S.A. 70:151-155(1973) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN FORMATION OF THE EF-G/RIBOSOME COMPLEX.
      Strain: B/2.
    7. "The ribosomal neighbourhood of the central fold of tRNA: cross-links from position 47 of tRNA located at the A, P or E site."
      Osswald M., Doering T., Brimacombe R.
      Nucleic Acids Res. 23:4635-4641(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CROSS-LINKING TO THE TRNA CENTRAL FOLD.
      Strain: MRE-600.
    8. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    9. Cited for: ROLE IN P SITE TRNA-BINDING, MUTAGENESIS.
      Strain: CSH142.
    10. "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.
    11. "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.
    12. "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.
    13. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
      Strain: MRE-600.

    Entry informationi

    Entry nameiRS9_ECOLI
    AccessioniPrimary (citable) accession number: P0A7X3
    Secondary accession number(s): P02363, Q2M8Y3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 99 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