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P0A7V0

- RS2_ECOLI

UniProt

P0A7V0 - RS2_ECOLI

Protein

30S ribosomal protein S2

Gene

rpsB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 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

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. structural constituent of ribosome Source: InterPro
    3. zinc ion binding Source: EcoliWiki

    GO - Biological processi

    1. translation Source: InterPro

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10901-MONOMER.
    ECOL316407:JW0164-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    30S ribosomal protein S2
    Gene namesi
    Name:rpsB
    Ordered Locus Names:b0169, JW0164
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10901. rpsB.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosolic small ribosomal subunit Source: EcoCyc

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 24124030S ribosomal protein S2PRO_0000134165Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei115 – 1151N6-succinyllysine1 Publication

    Proteomic databases

    PaxDbiP0A7V0.
    PRIDEiP0A7V0.

    2D gel databases

    SWISS-2DPAGEP0A7V0.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A7V0.

    Interactioni

    Subunit structurei

    Part of the 30S ribosomal subunit. Some nascent polypeptide chains are able to cross-link to this protein in situ.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    hslRP0ACG82EBI-543439,EBI-562824

    Protein-protein interaction databases

    BioGridi852185. 1 interaction.
    DIPiDIP-6877N.
    IntActiP0A7V0. 206 interactions.
    STRINGi511145.b0169.

    Structurei

    Secondary structure

    1
    241
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni10 – 156
    Beta strandi19 – 213
    Helixi25 – 273
    Helixi28 – 303
    Beta strandi31 – 333
    Beta strandi35 – 373
    Beta strandi38 – 403
    Helixi43 – 6018
    Turni61 – 633
    Beta strandi67 – 704
    Turni74 – 763
    Turni78 – 803
    Beta strandi81 – 833
    Turni84 – 863
    Beta strandi87 – 893
    Beta strandi91 – 944
    Turni98 – 1036
    Helixi104 – 11815
    Beta strandi119 – 1246
    Beta strandi126 – 1294
    Turni132 – 1343
    Helixi135 – 14511
    Beta strandi146 – 1483
    Turni150 – 1534
    Beta strandi159 – 1657
    Helixi166 – 1694
    Helixi170 – 1789
    Beta strandi183 – 1864
    Beta strandi189 – 1913
    Helixi193 – 1953
    Beta strandi197 – 2004
    Beta strandi204 – 2063
    Helixi207 – 21812
    Turni219 – 2224
    Turni223 – 2253

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M5Gmodel-B6-214[»]
    1P87electron microscopy11.50B2-241[»]
    1VS5X-ray3.46B1-241[»]
    1VS7X-ray3.46B1-241[»]
    2AVYX-ray3.46B2-241[»]
    2AW7X-ray3.46B2-241[»]
    2GY9electron microscopy15.00B6-241[»]
    2GYBelectron microscopy15.00B6-241[»]
    2I2PX-ray3.22B2-241[»]
    2I2UX-ray3.22B2-241[»]
    2QALX-ray3.21B2-241[»]
    2QANX-ray3.21B2-241[»]
    2QB9X-ray3.54B2-241[»]
    2QBBX-ray3.54B2-241[»]
    2QBDX-ray3.30B2-241[»]
    2QBFX-ray3.30B2-241[»]
    2QBHX-ray4.00B2-241[»]
    2QBJX-ray4.00B2-241[»]
    2QOUX-ray3.93B2-241[»]
    2QOWX-ray3.93B2-241[»]
    2QOYX-ray3.50B2-241[»]
    2QP0X-ray3.50B2-241[»]
    2VHOX-ray3.74B2-241[»]
    2VHPX-ray3.74B2-241[»]
    2WWLelectron microscopy5.80B9-226[»]
    2YKRelectron microscopy9.80B9-226[»]
    2Z4KX-ray4.45B2-241[»]
    2Z4MX-ray4.45B2-241[»]
    3DF1X-ray3.50B2-241[»]
    3DF3X-ray3.50B2-240[»]
    3E1Aelectron microscopy-B1-241[»]
    3E1Celectron microscopy-B1-241[»]
    3FIHelectron microscopy6.70B9-226[»]
    3I1MX-ray3.19B1-241[»]
    3I1OX-ray3.19B1-241[»]
    3I1QX-ray3.81B1-241[»]
    3I1SX-ray3.81B1-241[»]
    3I1ZX-ray3.71B1-241[»]
    3I21X-ray3.71B1-241[»]
    3IZVelectron microscopy-F1-241[»]
    3IZWelectron microscopy-F1-241[»]
    3J00electron microscopy-B2-241[»]
    3J0Uelectron microscopy12.10E2-241[»]
    3J0Velectron microscopy14.70E2-241[»]
    3J0Xelectron microscopy13.50E2-241[»]
    3J0Zelectron microscopy11.50E2-241[»]
    3J10electron microscopy11.50E2-241[»]
    3J13electron microscopy13.10D2-241[»]
    3J18electron microscopy8.30B9-226[»]
    3J36electron microscopy9.80B2-241[»]
    3J4Velectron microscopy12.00B9-226[»]
    3J4Welectron microscopy12.00B9-226[»]
    3J4Yelectron microscopy17.00B9-226[»]
    3J4Zelectron microscopy20.00B9-226[»]
    3J53electron microscopy13.00B9-226[»]
    3J55electron microscopy15.00B9-226[»]
    3J57electron microscopy17.00B9-226[»]
    3J59electron microscopy12.00B9-226[»]
    3J5Belectron microscopy17.00B9-226[»]
    3J5Delectron microscopy17.00B9-226[»]
    3J5Felectron microscopy20.00B9-226[»]
    3J5Helectron microscopy15.00B9-226[»]
    3J5Jelectron microscopy9.00B9-226[»]
    3J5Nelectron microscopy6.80B1-241[»]
    3J5Telectron microscopy7.60B2-241[»]
    3J5Xelectron microscopy7.60B2-241[»]
    3KC4electron microscopy-B1-241[»]
    3OAQX-ray3.25B9-226[»]
    3OARX-ray3.25B9-226[»]
    3OFAX-ray3.19B9-226[»]
    3OFBX-ray3.19B9-226[»]
    3OFOX-ray3.10B9-226[»]
    3OFPX-ray3.10B9-226[»]
    3OFXX-ray3.29B9-226[»]
    3OFYX-ray3.29B9-226[»]
    3OR9X-ray3.30B1-241[»]
    3ORAX-ray3.30B1-241[»]
    3SFSX-ray3.20B1-241[»]
    3UOQX-ray3.70B1-241[»]
    4A2Ielectron microscopy16.50B9-226[»]
    4ADVelectron microscopy13.50B2-241[»]
    4GAQX-ray3.30B1-241[»]
    4GASX-ray3.30B1-241[»]
    4GD1X-ray3.00B9-226[»]
    4GD2X-ray3.00B9-226[»]
    4KIYX-ray2.90B1-241[»]
    4KJ0X-ray2.90B1-241[»]
    4KJ2X-ray2.90B1-241[»]
    4KJ4X-ray2.90B1-241[»]
    4KJ6X-ray2.90B1-241[»]
    4KJ8X-ray2.90B1-241[»]
    4KJAX-ray2.90B1-241[»]
    4KJCX-ray2.90B1-241[»]
    ProteinModelPortaliP0A7V0.
    SMRiP0A7V0. Positions 2-241.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A7V0.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein S2P family.Curated

    Phylogenomic databases

    eggNOGiCOG0052.
    HOGENOMiHOG000071892.
    KOiK02967.
    OMAiFVNYRWL.
    OrthoDBiEOG6XWV6P.
    PhylomeDBiP0A7V0.

    Family and domain databases

    HAMAPiMF_00291_B. Ribosomal_S2_B.
    InterProiIPR001865. Ribosomal_S2.
    IPR005706. Ribosomal_S2_bac/mit/plastid.
    IPR018130. Ribosomal_S2_CS.
    IPR023591. Ribosomal_S2_flav_dom.
    [Graphical view]
    PANTHERiPTHR12534. PTHR12534. 1 hit.
    PfamiPF00318. Ribosomal_S2. 1 hit.
    [Graphical view]
    PRINTSiPR00395. RIBOSOMALS2.
    SUPFAMiSSF52313. SSF52313. 1 hit.
    TIGRFAMsiTIGR01011. rpsB_bact. 1 hit.
    PROSITEiPS00962. RIBOSOMAL_S2_1. 1 hit.
    PS00963. RIBOSOMAL_S2_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0A7V0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATVSMRDML KAGVHFGHQT RYWNPKMKPF IFGARNKVHI INLEKTVPMF    50
    NEALAELNKI ASRKGKILFV GTKRAASEAV KDAALSCDQF FVNHRWLGGM 100
    LTNWKTVRQS IKRLKDLETQ SQDGTFDKLT KKEALMRTRE LEKLENSLGG 150
    IKDMGGLPDA LFVIDADHEH IAIKEANNLG IPVFAIVDTN SDPDGVDFVI 200
    PGNDDAIRAV TLYLGAVAAT VREGRSQDLA SQAEESFVEA E 241
    Length:241
    Mass (Da):26,744
    Last modified:January 23, 2007 - v2
    Checksum:i87A38C696115212E
    GO

    Mass spectrometryi

    Molecular mass is 26610.5 Da from positions 2 - 241. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00343 Genomic DNA. Translation: CAA23631.1.
    U70214 Genomic DNA. Translation: AAB08598.1.
    U00096 Genomic DNA. Translation: AAC73280.1.
    AP009048 Genomic DNA. Translation: BAB96744.1.
    PIRiA02696. R3EC2.
    RefSeqiNP_414711.1. NC_000913.3.
    YP_488471.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73280; AAC73280; b0169.
    BAB96744; BAB96744; BAB96744.
    GeneIDi12931818.
    947874.
    KEGGiecj:Y75_p0165.
    eco:b0169.
    PATRICi32115445. VBIEscCol129921_0174.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00343 Genomic DNA. Translation: CAA23631.1 .
    U70214 Genomic DNA. Translation: AAB08598.1 .
    U00096 Genomic DNA. Translation: AAC73280.1 .
    AP009048 Genomic DNA. Translation: BAB96744.1 .
    PIRi A02696. R3EC2.
    RefSeqi NP_414711.1. NC_000913.3.
    YP_488471.1. 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 - B 6-214 [» ]
    1P87 electron microscopy 11.50 B 2-241 [» ]
    1VS5 X-ray 3.46 B 1-241 [» ]
    1VS7 X-ray 3.46 B 1-241 [» ]
    2AVY X-ray 3.46 B 2-241 [» ]
    2AW7 X-ray 3.46 B 2-241 [» ]
    2GY9 electron microscopy 15.00 B 6-241 [» ]
    2GYB electron microscopy 15.00 B 6-241 [» ]
    2I2P X-ray 3.22 B 2-241 [» ]
    2I2U X-ray 3.22 B 2-241 [» ]
    2QAL X-ray 3.21 B 2-241 [» ]
    2QAN X-ray 3.21 B 2-241 [» ]
    2QB9 X-ray 3.54 B 2-241 [» ]
    2QBB X-ray 3.54 B 2-241 [» ]
    2QBD X-ray 3.30 B 2-241 [» ]
    2QBF X-ray 3.30 B 2-241 [» ]
    2QBH X-ray 4.00 B 2-241 [» ]
    2QBJ X-ray 4.00 B 2-241 [» ]
    2QOU X-ray 3.93 B 2-241 [» ]
    2QOW X-ray 3.93 B 2-241 [» ]
    2QOY X-ray 3.50 B 2-241 [» ]
    2QP0 X-ray 3.50 B 2-241 [» ]
    2VHO X-ray 3.74 B 2-241 [» ]
    2VHP X-ray 3.74 B 2-241 [» ]
    2WWL electron microscopy 5.80 B 9-226 [» ]
    2YKR electron microscopy 9.80 B 9-226 [» ]
    2Z4K X-ray 4.45 B 2-241 [» ]
    2Z4M X-ray 4.45 B 2-241 [» ]
    3DF1 X-ray 3.50 B 2-241 [» ]
    3DF3 X-ray 3.50 B 2-240 [» ]
    3E1A electron microscopy - B 1-241 [» ]
    3E1C electron microscopy - B 1-241 [» ]
    3FIH electron microscopy 6.70 B 9-226 [» ]
    3I1M X-ray 3.19 B 1-241 [» ]
    3I1O X-ray 3.19 B 1-241 [» ]
    3I1Q X-ray 3.81 B 1-241 [» ]
    3I1S X-ray 3.81 B 1-241 [» ]
    3I1Z X-ray 3.71 B 1-241 [» ]
    3I21 X-ray 3.71 B 1-241 [» ]
    3IZV electron microscopy - F 1-241 [» ]
    3IZW electron microscopy - F 1-241 [» ]
    3J00 electron microscopy - B 2-241 [» ]
    3J0U electron microscopy 12.10 E 2-241 [» ]
    3J0V electron microscopy 14.70 E 2-241 [» ]
    3J0X electron microscopy 13.50 E 2-241 [» ]
    3J0Z electron microscopy 11.50 E 2-241 [» ]
    3J10 electron microscopy 11.50 E 2-241 [» ]
    3J13 electron microscopy 13.10 D 2-241 [» ]
    3J18 electron microscopy 8.30 B 9-226 [» ]
    3J36 electron microscopy 9.80 B 2-241 [» ]
    3J4V electron microscopy 12.00 B 9-226 [» ]
    3J4W electron microscopy 12.00 B 9-226 [» ]
    3J4Y electron microscopy 17.00 B 9-226 [» ]
    3J4Z electron microscopy 20.00 B 9-226 [» ]
    3J53 electron microscopy 13.00 B 9-226 [» ]
    3J55 electron microscopy 15.00 B 9-226 [» ]
    3J57 electron microscopy 17.00 B 9-226 [» ]
    3J59 electron microscopy 12.00 B 9-226 [» ]
    3J5B electron microscopy 17.00 B 9-226 [» ]
    3J5D electron microscopy 17.00 B 9-226 [» ]
    3J5F electron microscopy 20.00 B 9-226 [» ]
    3J5H electron microscopy 15.00 B 9-226 [» ]
    3J5J electron microscopy 9.00 B 9-226 [» ]
    3J5N electron microscopy 6.80 B 1-241 [» ]
    3J5T electron microscopy 7.60 B 2-241 [» ]
    3J5X electron microscopy 7.60 B 2-241 [» ]
    3KC4 electron microscopy - B 1-241 [» ]
    3OAQ X-ray 3.25 B 9-226 [» ]
    3OAR X-ray 3.25 B 9-226 [» ]
    3OFA X-ray 3.19 B 9-226 [» ]
    3OFB X-ray 3.19 B 9-226 [» ]
    3OFO X-ray 3.10 B 9-226 [» ]
    3OFP X-ray 3.10 B 9-226 [» ]
    3OFX X-ray 3.29 B 9-226 [» ]
    3OFY X-ray 3.29 B 9-226 [» ]
    3OR9 X-ray 3.30 B 1-241 [» ]
    3ORA X-ray 3.30 B 1-241 [» ]
    3SFS X-ray 3.20 B 1-241 [» ]
    3UOQ X-ray 3.70 B 1-241 [» ]
    4A2I electron microscopy 16.50 B 9-226 [» ]
    4ADV electron microscopy 13.50 B 2-241 [» ]
    4GAQ X-ray 3.30 B 1-241 [» ]
    4GAS X-ray 3.30 B 1-241 [» ]
    4GD1 X-ray 3.00 B 9-226 [» ]
    4GD2 X-ray 3.00 B 9-226 [» ]
    4KIY X-ray 2.90 B 1-241 [» ]
    4KJ0 X-ray 2.90 B 1-241 [» ]
    4KJ2 X-ray 2.90 B 1-241 [» ]
    4KJ4 X-ray 2.90 B 1-241 [» ]
    4KJ6 X-ray 2.90 B 1-241 [» ]
    4KJ8 X-ray 2.90 B 1-241 [» ]
    4KJA X-ray 2.90 B 1-241 [» ]
    4KJC X-ray 2.90 B 1-241 [» ]
    ProteinModelPortali P0A7V0.
    SMRi P0A7V0. Positions 2-241.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 852185. 1 interaction.
    DIPi DIP-6877N.
    IntActi P0A7V0. 206 interactions.
    STRINGi 511145.b0169.

    Chemistry

    ChEMBLi CHEMBL2363135.

    2D gel databases

    SWISS-2DPAGE P0A7V0.

    Proteomic databases

    PaxDbi P0A7V0.
    PRIDEi P0A7V0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73280 ; AAC73280 ; b0169 .
    BAB96744 ; BAB96744 ; BAB96744 .
    GeneIDi 12931818.
    947874.
    KEGGi ecj:Y75_p0165.
    eco:b0169.
    PATRICi 32115445. VBIEscCol129921_0174.

    Organism-specific databases

    EchoBASEi EB0894.
    EcoGenei EG10901. rpsB.

    Phylogenomic databases

    eggNOGi COG0052.
    HOGENOMi HOG000071892.
    KOi K02967.
    OMAi FVNYRWL.
    OrthoDBi EOG6XWV6P.
    PhylomeDBi P0A7V0.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10901-MONOMER.
    ECOL316407:JW0164-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A7V0.
    PROi P0A7V0.

    Gene expression databases

    Genevestigatori P0A7V0.

    Family and domain databases

    HAMAPi MF_00291_B. Ribosomal_S2_B.
    InterProi IPR001865. Ribosomal_S2.
    IPR005706. Ribosomal_S2_bac/mit/plastid.
    IPR018130. Ribosomal_S2_CS.
    IPR023591. Ribosomal_S2_flav_dom.
    [Graphical view ]
    PANTHERi PTHR12534. PTHR12534. 1 hit.
    Pfami PF00318. Ribosomal_S2. 1 hit.
    [Graphical view ]
    PRINTSi PR00395. RIBOSOMALS2.
    SUPFAMi SSF52313. SSF52313. 1 hit.
    TIGRFAMsi TIGR01011. rpsB_bact. 1 hit.
    PROSITEi PS00962. RIBOSOMAL_S2_1. 1 hit.
    PS00963. RIBOSOMAL_S2_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Organization and nucleotide sequence of a new ribosomal operon in Escherichia coli containing the genes for ribosomal protein S2 and elongation factor Ts."
      An G., Bendiak D.S., Mamelak L.A., Friesen J.D.
      Nucleic Acids Res. 9:4163-4172(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
      Fujita N., Mori H., Yura T., Ishihama A.
      Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. "Sequence of minutes 4-25 of Escherichia coli."
      Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "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.
    6. "Primary structure of protein S2 from the Escherichia coli ribosome."
      Wittmann-Liebold B., Bosserhoff A.
      FEBS Lett. 129:10-16(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-241.
      Strain: K12.
    7. "Identification of Escherichia coli proteins cross-reacting with antibodies against region 2.2 peptide of RNA polymerase sigma subunit."
      Ueshima R., Fujita N., Ishihama A.
      Biochem. Biophys. Res. Commun. 184:634-639(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-31.
    8. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-13.
      Strain: K12 / EMG2.
    9. "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 27-35, CROSS-LINKING TO RRNA.
      Strain: MRE-600.
    10. "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.
    11. "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.
    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. "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.
    14. "Identification of lysine succinylation as a new post-translational modification."
      Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.
      Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION AT LYS-115.
      Strain: K12.
    15. "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.
    16. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
      Strain: MRE-600.

    Entry informationi

    Entry nameiRS2_ECOLI
    AccessioniPrimary (citable) accession number: P0A7V0
    Secondary accession number(s): P02351, Q9R2E5
    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