Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P02358

- RS6_ECOLI

UniProt

P02358 - RS6_ECOLI

Protein

30S ribosomal protein S6

Gene

rpsF

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

    Binds together with S18 to 16S ribosomal RNA.

    GO - Molecular functioni

    1. mRNA 5'-UTR binding Source: EcoCyc
    2. protein binding Source: IntAct
    3. small ribosomal subunit rRNA binding Source: EcoCyc
    4. structural constituent of ribosome Source: InterPro

    GO - Biological processi

    1. translation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    RNA-binding, rRNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10905-MONOMER.
    ECOL316407:JW4158-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    30S ribosomal protein S6
    Cleaved into the following 2 chains:
    Gene namesi
    Name:rpsF
    Ordered Locus Names:b4200, JW4158
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10905. rpsF.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosolic small ribosomal subunit Source: EcoCyc

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13513530S ribosomal protein S6, fully modified isoformPRO_0000030640Add
    BLAST
    Chaini1 – 13113130S ribosomal protein S6, non-modified isoformPRO_0000030641Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei93 – 931N6-acetyllysine1 Publication

    Post-translational modificationi

    5 different forms of the protein, varying only in the number of C-terminal glutamate residues, were isolated. The sequence shown is form S6-6, which is the longest. The first two Glu are encoded by the rpsF gene, the other Glu are added post-translationally by the RimK enzyme.

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP02358.
    PRIDEiP02358.

    2D gel databases

    SWISS-2DPAGEP02358.

    Expressioni

    Gene expression databases

    GenevestigatoriP02358.

    Interactioni

    Subunit structurei

    Part of the 30S ribosomal subunit. Interacts weakly with L2 in one of the 3.5 A resolved structures (PubMed:16272117).1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    rpsRP0A7T74EBI-543068,EBI-548844

    Protein-protein interaction databases

    DIPiDIP-10782N.
    IntActiP02358. 57 interactions.
    MINTiMINT-1279331.
    STRINGi511145.b4200.

    Structurei

    Secondary structure

    1
    135
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 43
    Beta strandi7 – 104
    Helixi12 – 176
    Helixi18 – 3114
    Beta strandi35 – 373
    Beta strandi40 – 456
    Beta strandi53 – 553
    Beta strandi57 – 615
    Beta strandi64 – 663
    Helixi68 – 8013
    Beta strandi82 – 865
    Beta strandi88 – 903

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EG0electron microscopy11.50C1-97[»]
    1M5Gmodel-F1-100[»]
    1P6Gelectron microscopy12.30F1-135[»]
    1P87electron microscopy11.50F1-135[»]
    1VS5X-ray3.46F1-135[»]
    1VS7X-ray3.46F1-135[»]
    2AVYX-ray3.46F1-135[»]
    2AW7X-ray3.46F1-135[»]
    2GY9electron microscopy15.00F1-95[»]
    2GYBelectron microscopy15.00F1-95[»]
    2I2PX-ray3.22F1-135[»]
    2I2UX-ray3.22F1-135[»]
    2QALX-ray3.21F1-135[»]
    2QANX-ray3.21F1-135[»]
    2QB9X-ray3.54F1-135[»]
    2QBBX-ray3.54F1-135[»]
    2QBDX-ray3.30F1-135[»]
    2QBFX-ray3.30F1-135[»]
    2QBHX-ray4.00F1-135[»]
    2QBJX-ray4.00F1-135[»]
    2QOUX-ray3.93F1-135[»]
    2QOWX-ray3.93F1-135[»]
    2QOYX-ray3.50F1-135[»]
    2QP0X-ray3.50F1-135[»]
    2VHOX-ray3.74F1-135[»]
    2VHPX-ray3.74F1-135[»]
    2WWLelectron microscopy5.80F1-100[»]
    2YKRelectron microscopy9.80F1-100[»]
    2Z4KX-ray4.45F1-135[»]
    2Z4MX-ray4.45F1-135[»]
    3DF1X-ray3.50F1-135[»]
    3DF3X-ray3.50F1-135[»]
    3E1Aelectron microscopy-T1-135[»]
    3E1Celectron microscopy-T1-135[»]
    3FIHelectron microscopy6.70F1-100[»]
    3I1MX-ray3.19F1-135[»]
    3I1OX-ray3.19F1-135[»]
    3I1QX-ray3.81F1-135[»]
    3I1SX-ray3.81F1-135[»]
    3I1ZX-ray3.71F1-135[»]
    3I21X-ray3.71F1-135[»]
    3IY8electron microscopy14.10F2-100[»]
    3IZVelectron microscopy-J1-135[»]
    3IZWelectron microscopy-J1-135[»]
    3J00electron microscopy-F1-135[»]
    3J0Uelectron microscopy12.10I1-135[»]
    3J0Velectron microscopy14.70I1-135[»]
    3J0Xelectron microscopy13.50I1-135[»]
    3J0Zelectron microscopy11.50I1-135[»]
    3J10electron microscopy11.50I1-135[»]
    3J13electron microscopy13.10H1-135[»]
    3J18electron microscopy8.30F1-100[»]
    3J36electron microscopy9.80F1-135[»]
    3J4Velectron microscopy12.00F1-100[»]
    3J4Welectron microscopy12.00F1-100[»]
    3J4Yelectron microscopy17.00F1-100[»]
    3J4Zelectron microscopy20.00F1-100[»]
    3J53electron microscopy13.00F1-100[»]
    3J55electron microscopy15.00F1-100[»]
    3J57electron microscopy17.00F1-100[»]
    3J59electron microscopy12.00F1-100[»]
    3J5Belectron microscopy17.00F1-100[»]
    3J5Delectron microscopy17.00F1-100[»]
    3J5Felectron microscopy20.00F1-100[»]
    3J5Helectron microscopy15.00F1-100[»]
    3J5Jelectron microscopy9.00F1-100[»]
    3J5Nelectron microscopy6.80F1-135[»]
    3J5Telectron microscopy7.60F1-131[»]
    3J5Xelectron microscopy7.60F1-131[»]
    3KC4electron microscopy-F1-135[»]
    3OAQX-ray3.25F1-100[»]
    3OARX-ray3.25F1-100[»]
    3OFAX-ray3.19F1-100[»]
    3OFBX-ray3.19F1-100[»]
    3OFOX-ray3.10F1-100[»]
    3OFPX-ray3.10F1-100[»]
    3OFXX-ray3.29F1-100[»]
    3OFYX-ray3.29F1-100[»]
    3OR9X-ray3.30F1-135[»]
    3ORAX-ray3.30F1-135[»]
    3SFSX-ray3.20F1-131[»]
    3UOQX-ray3.70F1-135[»]
    4A2Ielectron microscopy16.50F1-100[»]
    4ADVelectron microscopy13.50F1-135[»]
    4GAQX-ray3.30F1-135[»]
    4GASX-ray3.30F1-135[»]
    4GD1X-ray3.00F1-100[»]
    4GD2X-ray3.00F1-100[»]
    4KIYX-ray2.90F1-135[»]
    4KJ0X-ray2.90F1-135[»]
    4KJ2X-ray2.90F1-135[»]
    4KJ4X-ray2.90F1-135[»]
    4KJ6X-ray2.90F1-135[»]
    4KJ8X-ray2.90F1-135[»]
    4KJAX-ray2.90F1-135[»]
    4KJCX-ray2.90F1-135[»]
    ProteinModelPortaliP02358.
    SMRiP02358. Positions 1-129.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02358.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein S6P family.Curated

    Phylogenomic databases

    eggNOGiCOG0360.
    HOGENOMiHOG000040438.
    KOiK02990.
    OMAiIRNMIMR.
    PhylomeDBiP02358.

    Family and domain databases

    Gene3Di3.30.70.60. 1 hit.
    HAMAPiMF_00360. Ribosomal_S6.
    InterProiIPR000529. Ribosomal_S6.
    IPR020815. Ribosomal_S6_CS.
    IPR020814. Ribosomal_S6_plastid/chlpt.
    IPR014717. Transl_elong_EF1B/ribosomal_S6.
    [Graphical view]
    PfamiPF01250. Ribosomal_S6. 1 hit.
    [Graphical view]
    SUPFAMiSSF54995. SSF54995. 1 hit.
    TIGRFAMsiTIGR00166. S6. 1 hit.
    PROSITEiPS01048. RIBOSOMAL_S6. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P02358-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRHYEIVFMV HPDQSEQVPG MIERYTAAIT GAEGKIHRLE DWGRRQLAYP    50
    INKLHKAHYV LMNVEAPQEV IDELETTFRF NDAVIRSMVM RTKHAVTEAS 100
    PMVKAKDERR ERRDDFANET ADDAEAGDSE EEEEE 135
    Length:135
    Mass (Da):15,703
    Last modified:July 21, 1986 - v1
    Checksum:iF4CC629711C1FD0E
    GO

    Sequence cautioni

    The sequence AAA97096.1 differs from that shown. Reason: Up to 4 Glu residues can be added post-translationally.
    The sequence AAC77157.5 differs from that shown. Reason: Up to 4 Glu residues can be added post-translationally.
    The sequence BAE78201.1 differs from that shown. Reason: Up to 4 Glu residues can be added post-translationally.
    The sequence CAA27652.1 differs from that shown. Reason: Up to 4 Glu residues can be added post-translationally.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 141Q → T AA sequence (PubMed:9868784)Curated
    Sequence conflicti20 – 201G → A AA sequence (PubMed:9868784)Curated

    Mass spectrometryi

    Molecular mass is 15187.2 Da from positions 1 - 131. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04022 Genomic DNA. Translation: CAA27652.1. Sequence problems.
    U14003 Genomic DNA. Translation: AAA97096.1. Sequence problems.
    U00096 Genomic DNA. Translation: AAC77157.5. Sequence problems.
    AP009048 Genomic DNA. Translation: BAE78201.1. Sequence problems.
    PIRiC65231. R3EC6.
    RefSeqiNP_418621.5. NC_000913.3.
    YP_492342.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77157; AAC77157; b4200.
    BAE78201; BAE78201; BAE78201.
    GeneIDi12930647.
    948723.
    KEGGiecj:Y75_p4086.
    eco:b4200.
    PATRICi48667972. VBIEscCol107702_4239.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04022 Genomic DNA. Translation: CAA27652.1 . Sequence problems.
    U14003 Genomic DNA. Translation: AAA97096.1 . Sequence problems.
    U00096 Genomic DNA. Translation: AAC77157.5 . Sequence problems.
    AP009048 Genomic DNA. Translation: BAE78201.1 . Sequence problems.
    PIRi C65231. R3EC6.
    RefSeqi NP_418621.5. NC_000913.3.
    YP_492342.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EG0 electron microscopy 11.50 C 1-97 [» ]
    1M5G model - F 1-100 [» ]
    1P6G electron microscopy 12.30 F 1-135 [» ]
    1P87 electron microscopy 11.50 F 1-135 [» ]
    1VS5 X-ray 3.46 F 1-135 [» ]
    1VS7 X-ray 3.46 F 1-135 [» ]
    2AVY X-ray 3.46 F 1-135 [» ]
    2AW7 X-ray 3.46 F 1-135 [» ]
    2GY9 electron microscopy 15.00 F 1-95 [» ]
    2GYB electron microscopy 15.00 F 1-95 [» ]
    2I2P X-ray 3.22 F 1-135 [» ]
    2I2U X-ray 3.22 F 1-135 [» ]
    2QAL X-ray 3.21 F 1-135 [» ]
    2QAN X-ray 3.21 F 1-135 [» ]
    2QB9 X-ray 3.54 F 1-135 [» ]
    2QBB X-ray 3.54 F 1-135 [» ]
    2QBD X-ray 3.30 F 1-135 [» ]
    2QBF X-ray 3.30 F 1-135 [» ]
    2QBH X-ray 4.00 F 1-135 [» ]
    2QBJ X-ray 4.00 F 1-135 [» ]
    2QOU X-ray 3.93 F 1-135 [» ]
    2QOW X-ray 3.93 F 1-135 [» ]
    2QOY X-ray 3.50 F 1-135 [» ]
    2QP0 X-ray 3.50 F 1-135 [» ]
    2VHO X-ray 3.74 F 1-135 [» ]
    2VHP X-ray 3.74 F 1-135 [» ]
    2WWL electron microscopy 5.80 F 1-100 [» ]
    2YKR electron microscopy 9.80 F 1-100 [» ]
    2Z4K X-ray 4.45 F 1-135 [» ]
    2Z4M X-ray 4.45 F 1-135 [» ]
    3DF1 X-ray 3.50 F 1-135 [» ]
    3DF3 X-ray 3.50 F 1-135 [» ]
    3E1A electron microscopy - T 1-135 [» ]
    3E1C electron microscopy - T 1-135 [» ]
    3FIH electron microscopy 6.70 F 1-100 [» ]
    3I1M X-ray 3.19 F 1-135 [» ]
    3I1O X-ray 3.19 F 1-135 [» ]
    3I1Q X-ray 3.81 F 1-135 [» ]
    3I1S X-ray 3.81 F 1-135 [» ]
    3I1Z X-ray 3.71 F 1-135 [» ]
    3I21 X-ray 3.71 F 1-135 [» ]
    3IY8 electron microscopy 14.10 F 2-100 [» ]
    3IZV electron microscopy - J 1-135 [» ]
    3IZW electron microscopy - J 1-135 [» ]
    3J00 electron microscopy - F 1-135 [» ]
    3J0U electron microscopy 12.10 I 1-135 [» ]
    3J0V electron microscopy 14.70 I 1-135 [» ]
    3J0X electron microscopy 13.50 I 1-135 [» ]
    3J0Z electron microscopy 11.50 I 1-135 [» ]
    3J10 electron microscopy 11.50 I 1-135 [» ]
    3J13 electron microscopy 13.10 H 1-135 [» ]
    3J18 electron microscopy 8.30 F 1-100 [» ]
    3J36 electron microscopy 9.80 F 1-135 [» ]
    3J4V electron microscopy 12.00 F 1-100 [» ]
    3J4W electron microscopy 12.00 F 1-100 [» ]
    3J4Y electron microscopy 17.00 F 1-100 [» ]
    3J4Z electron microscopy 20.00 F 1-100 [» ]
    3J53 electron microscopy 13.00 F 1-100 [» ]
    3J55 electron microscopy 15.00 F 1-100 [» ]
    3J57 electron microscopy 17.00 F 1-100 [» ]
    3J59 electron microscopy 12.00 F 1-100 [» ]
    3J5B electron microscopy 17.00 F 1-100 [» ]
    3J5D electron microscopy 17.00 F 1-100 [» ]
    3J5F electron microscopy 20.00 F 1-100 [» ]
    3J5H electron microscopy 15.00 F 1-100 [» ]
    3J5J electron microscopy 9.00 F 1-100 [» ]
    3J5N electron microscopy 6.80 F 1-135 [» ]
    3J5T electron microscopy 7.60 F 1-131 [» ]
    3J5X electron microscopy 7.60 F 1-131 [» ]
    3KC4 electron microscopy - F 1-135 [» ]
    3OAQ X-ray 3.25 F 1-100 [» ]
    3OAR X-ray 3.25 F 1-100 [» ]
    3OFA X-ray 3.19 F 1-100 [» ]
    3OFB X-ray 3.19 F 1-100 [» ]
    3OFO X-ray 3.10 F 1-100 [» ]
    3OFP X-ray 3.10 F 1-100 [» ]
    3OFX X-ray 3.29 F 1-100 [» ]
    3OFY X-ray 3.29 F 1-100 [» ]
    3OR9 X-ray 3.30 F 1-135 [» ]
    3ORA X-ray 3.30 F 1-135 [» ]
    3SFS X-ray 3.20 F 1-131 [» ]
    3UOQ X-ray 3.70 F 1-135 [» ]
    4A2I electron microscopy 16.50 F 1-100 [» ]
    4ADV electron microscopy 13.50 F 1-135 [» ]
    4GAQ X-ray 3.30 F 1-135 [» ]
    4GAS X-ray 3.30 F 1-135 [» ]
    4GD1 X-ray 3.00 F 1-100 [» ]
    4GD2 X-ray 3.00 F 1-100 [» ]
    4KIY X-ray 2.90 F 1-135 [» ]
    4KJ0 X-ray 2.90 F 1-135 [» ]
    4KJ2 X-ray 2.90 F 1-135 [» ]
    4KJ4 X-ray 2.90 F 1-135 [» ]
    4KJ6 X-ray 2.90 F 1-135 [» ]
    4KJ8 X-ray 2.90 F 1-135 [» ]
    4KJA X-ray 2.90 F 1-135 [» ]
    4KJC X-ray 2.90 F 1-135 [» ]
    ProteinModelPortali P02358.
    SMRi P02358. Positions 1-129.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10782N.
    IntActi P02358. 57 interactions.
    MINTi MINT-1279331.
    STRINGi 511145.b4200.

    Chemistry

    ChEMBLi CHEMBL2363135.

    2D gel databases

    SWISS-2DPAGE P02358.

    Proteomic databases

    PaxDbi P02358.
    PRIDEi P02358.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC77157 ; AAC77157 ; b4200 .
    BAE78201 ; BAE78201 ; BAE78201 .
    GeneIDi 12930647.
    948723.
    KEGGi ecj:Y75_p4086.
    eco:b4200.
    PATRICi 48667972. VBIEscCol107702_4239.

    Organism-specific databases

    EchoBASEi EB0898.
    EcoGenei EG10905. rpsF.

    Phylogenomic databases

    eggNOGi COG0360.
    HOGENOMi HOG000040438.
    KOi K02990.
    OMAi IRNMIMR.
    PhylomeDBi P02358.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10905-MONOMER.
    ECOL316407:JW4158-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P02358.
    PROi P02358.

    Gene expression databases

    Genevestigatori P02358.

    Family and domain databases

    Gene3Di 3.30.70.60. 1 hit.
    HAMAPi MF_00360. Ribosomal_S6.
    InterProi IPR000529. Ribosomal_S6.
    IPR020815. Ribosomal_S6_CS.
    IPR020814. Ribosomal_S6_plastid/chlpt.
    IPR014717. Transl_elong_EF1B/ribosomal_S6.
    [Graphical view ]
    Pfami PF01250. Ribosomal_S6. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54995. SSF54995. 1 hit.
    TIGRFAMsi TIGR00166. S6. 1 hit.
    PROSITEi PS01048. RIBOSOMAL_S6. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Determination of the complete amino-acid sequence of protein S6 from the wild-type and a mutant of Escherichia coli."
      Hitz H., Schaefer D., Wittmann-Liebold B.
      Eur. J. Biochem. 75:497-512(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
      Strain: K.
    2. "The nucleotide sequence of an Escherichia coli chromosomal region containing the genes for ribosomal proteins S6, S18, L9 and an open reading frame."
      Schnier J., Kitakawa M., Isono K.
      Mol. Gen. Genet. 204:126-132(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-131.
    3. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
      Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
      Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-131.
      Strain: K12 / MG1655 / ATCC 47076.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-131.
      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] OF 1-131.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "Small genes/gene-products in Escherichia coli K-12."
      Wasinger V.C., Humphery-Smith I.
      FEMS Microbiol. Lett. 169:375-382(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-20.
      Strain: K12.
    7. Cited for: PROTEIN SEQUENCE OF 1-11.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    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 1-12.
      Strain: K12 / EMG2.
    9. Cited for: PROTEIN SEQUENCE OF 1-4.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    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. "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.
    12. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
      Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
      Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-93, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
    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. "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.
    15. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
      Strain: MRE-600.

    Entry informationi

    Entry nameiRS6_ECOLI
    AccessioniPrimary (citable) accession number: P02358
    Secondary accession number(s): Q2M6A5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 159 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, 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