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P0A7W7

- RS8_ECOLI

UniProt

P0A7W7 - RS8_ECOLI

Protein

30S ribosomal protein S8

Gene

rpsH

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

    One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.By similarity
    Protein S8 is a translational repressor protein, it controls the translation of the spc operon by binding to its mRNA.

    GO - Molecular functioni

    1. rRNA binding Source: EcoliWiki
    2. structural constituent of ribosome Source: InterPro

    GO - Biological processi

    1. regulation of mRNA stability Source: EcoliWiki
    2. regulation of translation Source: UniProtKB-KW
    3. translation Source: InterPro

    Keywords - Molecular functioni

    Repressor, Ribonucleoprotein, Ribosomal protein

    Keywords - Biological processi

    Translation regulation

    Keywords - Ligandi

    RNA-binding, rRNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10907-MONOMER.
    ECOL316407:JW3268-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    30S ribosomal protein S8
    Gene namesi
    Name:rpsH
    Ordered Locus Names:b3306, JW3268
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10907. rpsH.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosolic small ribosomal subunit Source: EcoCyc

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 13012930S ribosomal protein S8PRO_0000126405Add
    BLAST

    Proteomic databases

    PaxDbiP0A7W7.
    PRIDEiP0A7W7.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A7W7.

    Interactioni

    Subunit structurei

    Part of the 30S ribosomal subunit. Contacts proteins S5 and S12 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi852114. 1 interaction.
    DIPiDIP-47901N.
    IntActiP0A7W7. 38 interactions.
    MINTiMINT-1318565.
    STRINGi511145.b3306.

    Structurei

    Secondary structure

    1
    130
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 1914
    Beta strandi23 – 286
    Helixi31 – 4212
    Beta strandi45 – 528
    Beta strandi54 – 563
    Beta strandi58 – 636
    Beta strandi65 – 717
    Beta strandi75 – 773
    Beta strandi81 – 833
    Helixi89 – 913
    Beta strandi97 – 993
    Beta strandi101 – 1066
    Beta strandi109 – 1124
    Helixi113 – 1197
    Beta strandi123 – 1297

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EG0electron microscopy11.50E1-130[»]
    1M5Gmodel-H2-130[»]
    1P6Gelectron microscopy12.30H2-130[»]
    1P87electron microscopy11.50H2-130[»]
    1S03X-ray2.70G/H2-130[»]
    1VS5X-ray3.46H1-130[»]
    1VS7X-ray3.46H1-130[»]
    2AVYX-ray3.46H2-130[»]
    2AW7X-ray3.46H2-130[»]
    2GY9electron microscopy15.00H3-129[»]
    2GYBelectron microscopy15.00H3-129[»]
    2I2PX-ray3.22H2-130[»]
    2I2UX-ray3.22H2-130[»]
    2QALX-ray3.21H2-130[»]
    2QANX-ray3.21H2-130[»]
    2QB9X-ray3.54H2-130[»]
    2QBBX-ray3.54H2-130[»]
    2QBDX-ray3.30H2-130[»]
    2QBFX-ray3.30H2-130[»]
    2QBHX-ray4.00H2-130[»]
    2QBJX-ray4.00H2-130[»]
    2QOUX-ray3.93H2-130[»]
    2QOWX-ray3.93H2-130[»]
    2QOYX-ray3.50H2-130[»]
    2QP0X-ray3.50H2-130[»]
    2VHOX-ray3.74H2-130[»]
    2VHPX-ray3.74H2-130[»]
    2WWLelectron microscopy5.80H2-130[»]
    2YKRelectron microscopy9.80H2-130[»]
    2Z4KX-ray4.45H2-130[»]
    2Z4MX-ray4.45H2-130[»]
    3DF1X-ray3.50H2-129[»]
    3DF3X-ray3.50H2-129[»]
    3E1Aelectron microscopy9.00V1-130[»]
    3E1Celectron microscopy9.00V1-130[»]
    3FIHelectron microscopy6.70H2-130[»]
    3I1MX-ray3.19H1-130[»]
    3I1OX-ray3.19H1-130[»]
    3I1QX-ray3.81H1-130[»]
    3I1SX-ray3.81H1-130[»]
    3I1ZX-ray3.71H1-130[»]
    3I21X-ray3.71H1-130[»]
    3IZVelectron microscopy-L1-130[»]
    3IZWelectron microscopy-L1-130[»]
    3J00electron microscopy-H2-130[»]
    3J0Uelectron microscopy12.10K2-130[»]
    3J0Velectron microscopy14.70K2-130[»]
    3J0Xelectron microscopy13.50K2-130[»]
    3J0Zelectron microscopy11.50K2-130[»]
    3J10electron microscopy11.50K2-130[»]
    3J13electron microscopy13.10J2-130[»]
    3J18electron microscopy8.30H2-130[»]
    3J36electron microscopy9.80H2-130[»]
    3J4Velectron microscopy12.00H1-130[»]
    3J4Welectron microscopy12.00H1-130[»]
    3J4Yelectron microscopy17.00H1-130[»]
    3J4Zelectron microscopy20.00H1-130[»]
    3J53electron microscopy13.00H1-130[»]
    3J55electron microscopy15.00H1-130[»]
    3J57electron microscopy17.00H1-130[»]
    3J59electron microscopy12.00H1-130[»]
    3J5Belectron microscopy17.00H1-130[»]
    3J5Delectron microscopy17.00H1-130[»]
    3J5Felectron microscopy20.00H1-130[»]
    3J5Helectron microscopy15.00H1-130[»]
    3J5Jelectron microscopy9.00H1-130[»]
    3J5Nelectron microscopy6.80H1-130[»]
    3J5Telectron microscopy7.60H2-130[»]
    3J5Xelectron microscopy7.60H2-130[»]
    3KC4electron microscopy-H1-130[»]
    3OAQX-ray3.25H2-130[»]
    3OARX-ray3.25H2-130[»]
    3OFAX-ray3.19H2-130[»]
    3OFBX-ray3.19H2-130[»]
    3OFOX-ray3.10H2-130[»]
    3OFPX-ray3.10H2-130[»]
    3OFXX-ray3.29H2-130[»]
    3OFYX-ray3.29H2-130[»]
    3OR9X-ray3.30H1-130[»]
    3ORAX-ray3.30H1-130[»]
    3SFSX-ray3.20H1-130[»]
    3UOQX-ray3.70H1-130[»]
    4A2Ielectron microscopy16.50H2-130[»]
    4ADVelectron microscopy13.50H2-130[»]
    4GAQX-ray3.30H1-130[»]
    4GASX-ray3.30H1-130[»]
    4GD1X-ray3.00H2-130[»]
    4GD2X-ray3.00H2-130[»]
    4KIYX-ray2.90H1-130[»]
    4KJ0X-ray2.90H1-130[»]
    4KJ2X-ray2.90H1-130[»]
    4KJ4X-ray2.90H1-130[»]
    4KJ6X-ray2.90H1-130[»]
    4KJ8X-ray2.90H1-130[»]
    4KJAX-ray2.90H1-130[»]
    4KJCX-ray2.90H1-130[»]
    ProteinModelPortaliP0A7W7.
    SMRiP0A7W7. Positions 3-129.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A7W7.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein S8P family.Curated

    Phylogenomic databases

    eggNOGiCOG0096.
    HOGENOMiHOG000204095.
    KOiK02994.
    OMAiTRVRNGQ.
    OrthoDBiEOG6Z0QH1.
    PhylomeDBiP0A7W7.

    Family and domain databases

    HAMAPiMF_01302_B. Ribosomal_S8_B.
    InterProiIPR000630. Ribosomal_S8.
    [Graphical view]
    PANTHERiPTHR11758. PTHR11758. 1 hit.
    PfamiPF00410. Ribosomal_S8. 1 hit.
    [Graphical view]
    SUPFAMiSSF56047. SSF56047. 1 hit.
    PROSITEiPS00053. RIBOSOMAL_S8. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0A7W7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSMQDPIADM LTRIRNGQAA NKAAVTMPSS KLKVAIANVL KEEGFIEDFK    50
    VEGDTKPELE LTLKYFQGKA VVESIQRVSR PGLRIYKRKD ELPKVMAGLG 100
    IAVVSTSKGV MTDRAARQAG LGGEIICYVA 130
    Length:130
    Mass (Da):14,127
    Last modified:January 23, 2007 - v2
    Checksum:i74641BC5021DA651
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti91 – 911E → Q in CAA25719. (PubMed:6222285)Curated

    Mass spectrometryi

    Molecular mass is 13993.2 Da from positions 2 - 130. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01563 Genomic DNA. Translation: CAA25719.1.
    U18997 Genomic DNA. Translation: AAA58103.1.
    U00096 Genomic DNA. Translation: AAC76331.1.
    AP009048 Genomic DNA. Translation: BAE77985.1.
    PIRiE65123. R3EC8.
    RefSeqiNP_417765.1. NC_000913.3.
    YP_492126.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76331; AAC76331; b3306.
    BAE77985; BAE77985; BAE77985.
    GeneIDi12934408.
    947802.
    KEGGiecj:Y75_p3870.
    eco:b3306.
    PATRICi32122044. VBIEscCol129921_3399.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01563 Genomic DNA. Translation: CAA25719.1 .
    U18997 Genomic DNA. Translation: AAA58103.1 .
    U00096 Genomic DNA. Translation: AAC76331.1 .
    AP009048 Genomic DNA. Translation: BAE77985.1 .
    PIRi E65123. R3EC8.
    RefSeqi NP_417765.1. NC_000913.3.
    YP_492126.1. 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 E 1-130 [» ]
    1M5G model - H 2-130 [» ]
    1P6G electron microscopy 12.30 H 2-130 [» ]
    1P87 electron microscopy 11.50 H 2-130 [» ]
    1S03 X-ray 2.70 G/H 2-130 [» ]
    1VS5 X-ray 3.46 H 1-130 [» ]
    1VS7 X-ray 3.46 H 1-130 [» ]
    2AVY X-ray 3.46 H 2-130 [» ]
    2AW7 X-ray 3.46 H 2-130 [» ]
    2GY9 electron microscopy 15.00 H 3-129 [» ]
    2GYB electron microscopy 15.00 H 3-129 [» ]
    2I2P X-ray 3.22 H 2-130 [» ]
    2I2U X-ray 3.22 H 2-130 [» ]
    2QAL X-ray 3.21 H 2-130 [» ]
    2QAN X-ray 3.21 H 2-130 [» ]
    2QB9 X-ray 3.54 H 2-130 [» ]
    2QBB X-ray 3.54 H 2-130 [» ]
    2QBD X-ray 3.30 H 2-130 [» ]
    2QBF X-ray 3.30 H 2-130 [» ]
    2QBH X-ray 4.00 H 2-130 [» ]
    2QBJ X-ray 4.00 H 2-130 [» ]
    2QOU X-ray 3.93 H 2-130 [» ]
    2QOW X-ray 3.93 H 2-130 [» ]
    2QOY X-ray 3.50 H 2-130 [» ]
    2QP0 X-ray 3.50 H 2-130 [» ]
    2VHO X-ray 3.74 H 2-130 [» ]
    2VHP X-ray 3.74 H 2-130 [» ]
    2WWL electron microscopy 5.80 H 2-130 [» ]
    2YKR electron microscopy 9.80 H 2-130 [» ]
    2Z4K X-ray 4.45 H 2-130 [» ]
    2Z4M X-ray 4.45 H 2-130 [» ]
    3DF1 X-ray 3.50 H 2-129 [» ]
    3DF3 X-ray 3.50 H 2-129 [» ]
    3E1A electron microscopy 9.00 V 1-130 [» ]
    3E1C electron microscopy 9.00 V 1-130 [» ]
    3FIH electron microscopy 6.70 H 2-130 [» ]
    3I1M X-ray 3.19 H 1-130 [» ]
    3I1O X-ray 3.19 H 1-130 [» ]
    3I1Q X-ray 3.81 H 1-130 [» ]
    3I1S X-ray 3.81 H 1-130 [» ]
    3I1Z X-ray 3.71 H 1-130 [» ]
    3I21 X-ray 3.71 H 1-130 [» ]
    3IZV electron microscopy - L 1-130 [» ]
    3IZW electron microscopy - L 1-130 [» ]
    3J00 electron microscopy - H 2-130 [» ]
    3J0U electron microscopy 12.10 K 2-130 [» ]
    3J0V electron microscopy 14.70 K 2-130 [» ]
    3J0X electron microscopy 13.50 K 2-130 [» ]
    3J0Z electron microscopy 11.50 K 2-130 [» ]
    3J10 electron microscopy 11.50 K 2-130 [» ]
    3J13 electron microscopy 13.10 J 2-130 [» ]
    3J18 electron microscopy 8.30 H 2-130 [» ]
    3J36 electron microscopy 9.80 H 2-130 [» ]
    3J4V electron microscopy 12.00 H 1-130 [» ]
    3J4W electron microscopy 12.00 H 1-130 [» ]
    3J4Y electron microscopy 17.00 H 1-130 [» ]
    3J4Z electron microscopy 20.00 H 1-130 [» ]
    3J53 electron microscopy 13.00 H 1-130 [» ]
    3J55 electron microscopy 15.00 H 1-130 [» ]
    3J57 electron microscopy 17.00 H 1-130 [» ]
    3J59 electron microscopy 12.00 H 1-130 [» ]
    3J5B electron microscopy 17.00 H 1-130 [» ]
    3J5D electron microscopy 17.00 H 1-130 [» ]
    3J5F electron microscopy 20.00 H 1-130 [» ]
    3J5H electron microscopy 15.00 H 1-130 [» ]
    3J5J electron microscopy 9.00 H 1-130 [» ]
    3J5N electron microscopy 6.80 H 1-130 [» ]
    3J5T electron microscopy 7.60 H 2-130 [» ]
    3J5X electron microscopy 7.60 H 2-130 [» ]
    3KC4 electron microscopy - H 1-130 [» ]
    3OAQ X-ray 3.25 H 2-130 [» ]
    3OAR X-ray 3.25 H 2-130 [» ]
    3OFA X-ray 3.19 H 2-130 [» ]
    3OFB X-ray 3.19 H 2-130 [» ]
    3OFO X-ray 3.10 H 2-130 [» ]
    3OFP X-ray 3.10 H 2-130 [» ]
    3OFX X-ray 3.29 H 2-130 [» ]
    3OFY X-ray 3.29 H 2-130 [» ]
    3OR9 X-ray 3.30 H 1-130 [» ]
    3ORA X-ray 3.30 H 1-130 [» ]
    3SFS X-ray 3.20 H 1-130 [» ]
    3UOQ X-ray 3.70 H 1-130 [» ]
    4A2I electron microscopy 16.50 H 2-130 [» ]
    4ADV electron microscopy 13.50 H 2-130 [» ]
    4GAQ X-ray 3.30 H 1-130 [» ]
    4GAS X-ray 3.30 H 1-130 [» ]
    4GD1 X-ray 3.00 H 2-130 [» ]
    4GD2 X-ray 3.00 H 2-130 [» ]
    4KIY X-ray 2.90 H 1-130 [» ]
    4KJ0 X-ray 2.90 H 1-130 [» ]
    4KJ2 X-ray 2.90 H 1-130 [» ]
    4KJ4 X-ray 2.90 H 1-130 [» ]
    4KJ6 X-ray 2.90 H 1-130 [» ]
    4KJ8 X-ray 2.90 H 1-130 [» ]
    4KJA X-ray 2.90 H 1-130 [» ]
    4KJC X-ray 2.90 H 1-130 [» ]
    ProteinModelPortali P0A7W7.
    SMRi P0A7W7. Positions 3-129.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 852114. 1 interaction.
    DIPi DIP-47901N.
    IntActi P0A7W7. 38 interactions.
    MINTi MINT-1318565.
    STRINGi 511145.b3306.

    Chemistry

    ChEMBLi CHEMBL2363135.

    Proteomic databases

    PaxDbi P0A7W7.
    PRIDEi P0A7W7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76331 ; AAC76331 ; b3306 .
    BAE77985 ; BAE77985 ; BAE77985 .
    GeneIDi 12934408.
    947802.
    KEGGi ecj:Y75_p3870.
    eco:b3306.
    PATRICi 32122044. VBIEscCol129921_3399.

    Organism-specific databases

    EchoBASEi EB0900.
    EcoGenei EG10907. rpsH.

    Phylogenomic databases

    eggNOGi COG0096.
    HOGENOMi HOG000204095.
    KOi K02994.
    OMAi TRVRNGQ.
    OrthoDBi EOG6Z0QH1.
    PhylomeDBi P0A7W7.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10907-MONOMER.
    ECOL316407:JW3268-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A7W7.
    PROi P0A7W7.

    Gene expression databases

    Genevestigatori P0A7W7.

    Family and domain databases

    HAMAPi MF_01302_B. Ribosomal_S8_B.
    InterProi IPR000630. Ribosomal_S8.
    [Graphical view ]
    PANTHERi PTHR11758. PTHR11758. 1 hit.
    Pfami PF00410. Ribosomal_S8. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56047. SSF56047. 1 hit.
    PROSITEi PS00053. RIBOSOMAL_S8. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene."
      Cerretti D.P., Dean D., Davis G.R., Bedwell D.M., Nomura M.
      Nucleic Acids Res. 11:2599-2616(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    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 amino acid sequence of the ribosomal protein S8 of Escherichia coli."
      Allen G., Wittmann-Liebold B.
      Hoppe-Seyler's Z. Physiol. Chem. 359:1509-1525(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-130.
      Strain: K.
    5. "Translational regulation by ribosomal protein S8 in Escherichia coli: structural homology between rRNA binding site and feedback target on mRNA."
      Olins P.O., Nomura M.
      Nucleic Acids Res. 9:1757-1764(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: MECHANISM OF TRANSLATION REGULATION.
    6. "Mutagenesis of ribosomal protein S8 from Escherichia coli: defects in regulation of the spc operon."
      Wower I., Kowaleski M.P., Sears L.E., Zimmermann R.A.
      J. Bacteriol. 174:1213-1221(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    7. "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.
    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 nameiRS8_ECOLI
    AccessioniPrimary (citable) accession number: P0A7W7
    Secondary accession number(s): P02361, Q2M6X1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 92 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