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P0ADZ4

- RS15_ECOLI

UniProt

P0ADZ4 - RS15_ECOLI

Protein

30S ribosomal protein S15

Gene

rpsO

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

    One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA.
    In the E.coli 70S ribosome it has been modeled (PubMed:12809609) to contact the 23S rRNA of the 50S subunit forming part of bridge B4. In the two 3.5 A resolved ribosome structures (PubMed:16272117) there are minor differences between side-chain conformations.2 Publications

    GO - Molecular functioni

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

    GO - Biological processi

    1. mRNA polyadenylation Source: EcoliWiki
    2. translation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    RNA-binding, rRNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10914-MONOMER.
    ECOL316407:JW3134-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    30S ribosomal protein S15UniRule annotation
    Gene namesi
    Name:rpsOUniRule annotation
    Synonyms:secC
    Ordered Locus Names:b3165, JW3134
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10914. rpsO.

    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 – 898830S ribosomal protein S15PRO_0000115437Add
    BLAST

    Proteomic databases

    PaxDbiP0ADZ4.
    PRIDEiP0ADZ4.

    Expressioni

    Gene expression databases

    GenevestigatoriP0ADZ4.

    Interactioni

    Subunit structurei

    Part of the 30S ribosomal subunit. Forms a bridge to the 50S subunit in the 70S ribosome, contacting the 23S rRNA.

    Protein-protein interaction databases

    DIPiDIP-47909N.
    IntActiP0ADZ4. 30 interactions.
    MINTiMINT-1299353.
    STRINGi511145.b3165.

    Structurei

    Secondary structure

    1
    89
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 1511
    Beta strandi16 – 183
    Helixi25 – 4218
    Helixi50 – 7324
    Helixi75 – 8410

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EG0electron microscopy11.50F1-89[»]
    1P6Gelectron microscopy12.30O2-89[»]
    1P87electron microscopy11.50O2-89[»]
    2AVYX-ray3.46O1-89[»]
    2AW7X-ray3.46O1-89[»]
    2GY9electron microscopy15.00O3-88[»]
    2GYBelectron microscopy15.00O3-88[»]
    2QALX-ray3.21O1-89[»]
    2QANX-ray3.21O1-89[»]
    2QB9X-ray3.54O1-89[»]
    2QBBX-ray3.54O1-89[»]
    2QBDX-ray3.30O1-89[»]
    2QBFX-ray3.30O1-89[»]
    2QBHX-ray4.00O1-89[»]
    2QBJX-ray4.00O1-89[»]
    2QOUX-ray3.93O1-89[»]
    2QOWX-ray3.93O1-89[»]
    2QOYX-ray3.50O1-89[»]
    2QP0X-ray3.50O1-89[»]
    2VAZelectron microscopy10.00F2-89[»]
    2WWLelectron microscopy5.80O2-89[»]
    2YKRelectron microscopy9.80O2-89[»]
    2Z4KX-ray4.45O1-89[»]
    2Z4MX-ray4.45O1-89[»]
    3DF1X-ray3.50O1-89[»]
    3DF3X-ray3.50O1-89[»]
    3E1Aelectron microscopy9.00H1-89[»]
    3E1Celectron microscopy9.00H1-89[»]
    3FIHelectron microscopy6.70O2-89[»]
    3I1MX-ray3.19O1-89[»]
    3I1OX-ray3.19O1-89[»]
    3I1QX-ray3.81O1-89[»]
    3I1SX-ray3.81O1-89[»]
    3I1ZX-ray3.71O1-89[»]
    3I21X-ray3.71O1-89[»]
    3IZVelectron microscopy-S1-89[»]
    3IZWelectron microscopy-S1-89[»]
    3J00electron microscopy-O2-89[»]
    3J18electron microscopy8.30O2-89[»]
    3J36electron microscopy9.80O2-89[»]
    3J4Velectron microscopy12.00O1-89[»]
    3J4Welectron microscopy12.00O1-89[»]
    3J4Yelectron microscopy17.00O1-89[»]
    3J4Zelectron microscopy20.00O1-89[»]
    3J53electron microscopy13.00O1-89[»]
    3J55electron microscopy15.00O1-89[»]
    3J57electron microscopy17.00O1-89[»]
    3J59electron microscopy12.00O1-89[»]
    3J5Belectron microscopy17.00O1-89[»]
    3J5Delectron microscopy17.00O1-89[»]
    3J5Felectron microscopy20.00O1-89[»]
    3J5Helectron microscopy15.00O1-89[»]
    3J5Jelectron microscopy9.00O1-89[»]
    3J5Nelectron microscopy6.80O1-89[»]
    3J5Telectron microscopy7.60O2-89[»]
    3J5Xelectron microscopy7.60O2-89[»]
    3KC4electron microscopy-O1-89[»]
    3OAQX-ray3.25O2-89[»]
    3OARX-ray3.25O2-89[»]
    3OFAX-ray3.19O2-89[»]
    3OFBX-ray3.19O2-89[»]
    3OFOX-ray3.10O2-89[»]
    3OFPX-ray3.10O2-89[»]
    3OFXX-ray3.29O2-89[»]
    3OFYX-ray3.29O2-89[»]
    3OR9X-ray3.30O1-89[»]
    3ORAX-ray3.30O1-89[»]
    3SFSX-ray3.20O1-89[»]
    3UOQX-ray3.70O1-89[»]
    4A2Ielectron microscopy16.50O2-89[»]
    4ADVelectron microscopy13.50O1-89[»]
    4GAQX-ray3.30O1-89[»]
    4GASX-ray3.30O1-89[»]
    4GD1X-ray3.00O2-89[»]
    4GD2X-ray3.00O2-89[»]
    4KIYX-ray2.90O1-89[»]
    4KJ0X-ray2.90O1-89[»]
    4KJ2X-ray2.90O1-89[»]
    4KJ4X-ray2.90O1-89[»]
    4KJ6X-ray2.90O1-89[»]
    4KJ8X-ray2.90O1-89[»]
    4KJAX-ray2.90O1-89[»]
    4KJCX-ray2.90O1-89[»]
    ProteinModelPortaliP0ADZ4.
    SMRiP0ADZ4. Positions 3-88.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0ADZ4.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein S15P family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0184.
    HOGENOMiHOG000040097.
    KOiK02956.
    OMAiNKQDHHS.
    OrthoDBiEOG6B368J.
    PhylomeDBiP0ADZ4.

    Family and domain databases

    Gene3Di1.10.287.10. 1 hit.
    HAMAPiMF_01343_B. Ribosomal_S15_B.
    InterProiIPR000589. Ribosomal_S15.
    IPR005290. Ribosomal_S15_bac-type.
    IPR009068. S15_NS1_RNA-bd.
    [Graphical view]
    PfamiPF00312. Ribosomal_S15. 1 hit.
    [Graphical view]
    SUPFAMiSSF47060. SSF47060. 1 hit.
    TIGRFAMsiTIGR00952. S15_bact. 1 hit.
    PROSITEiPS00362. RIBOSOMAL_S15. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0ADZ4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLSTEATAK IVSEFGRDAN DTGSTEVQVA LLTAQINHLQ GHFAEHKKDH   50
    HSRRGLLRMV SQRRKLLDYL KRKDVARYTQ LIERLGLRR 89
    Length:89
    Mass (Da):10,269
    Last modified:January 23, 2007 - v2
    Checksum:iAABDDA6674B99B1C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti66 – 661Missing(PubMed:3005122)Curated

    Mass spectrometryi

    Molecular mass is 10137.6 Da from positions 2 - 89. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01073 Genomic DNA. Translation: CAA25536.1.
    X00761 Genomic DNA. Translation: CAA25331.1.
    M14425 Genomic DNA. Translation: AAA24595.1.
    J02638 Genomic DNA. Translation: AAA83904.1.
    U18997 Genomic DNA. Translation: AAA57968.1.
    U00096 Genomic DNA. Translation: AAC76199.1.
    AP009048 Genomic DNA. Translation: BAE77211.1.
    X13775 Genomic DNA. Translation: CAA32022.1.
    PIRiB26118. R3EC15.
    RefSeqiNP_417634.1. NC_000913.3.
    YP_491352.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76199; AAC76199; b3165.
    BAE77211; BAE77211; BAE77211.
    GeneIDi12933439.
    947686.
    KEGGiecj:Y75_p3087.
    eco:b3165.
    PATRICi32121748. VBIEscCol129921_3260.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01073 Genomic DNA. Translation: CAA25536.1 .
    X00761 Genomic DNA. Translation: CAA25331.1 .
    M14425 Genomic DNA. Translation: AAA24595.1 .
    J02638 Genomic DNA. Translation: AAA83904.1 .
    U18997 Genomic DNA. Translation: AAA57968.1 .
    U00096 Genomic DNA. Translation: AAC76199.1 .
    AP009048 Genomic DNA. Translation: BAE77211.1 .
    X13775 Genomic DNA. Translation: CAA32022.1 .
    PIRi B26118. R3EC15.
    RefSeqi NP_417634.1. NC_000913.3.
    YP_491352.1. 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 F 1-89 [» ]
    1P6G electron microscopy 12.30 O 2-89 [» ]
    1P87 electron microscopy 11.50 O 2-89 [» ]
    2AVY X-ray 3.46 O 1-89 [» ]
    2AW7 X-ray 3.46 O 1-89 [» ]
    2GY9 electron microscopy 15.00 O 3-88 [» ]
    2GYB electron microscopy 15.00 O 3-88 [» ]
    2QAL X-ray 3.21 O 1-89 [» ]
    2QAN X-ray 3.21 O 1-89 [» ]
    2QB9 X-ray 3.54 O 1-89 [» ]
    2QBB X-ray 3.54 O 1-89 [» ]
    2QBD X-ray 3.30 O 1-89 [» ]
    2QBF X-ray 3.30 O 1-89 [» ]
    2QBH X-ray 4.00 O 1-89 [» ]
    2QBJ X-ray 4.00 O 1-89 [» ]
    2QOU X-ray 3.93 O 1-89 [» ]
    2QOW X-ray 3.93 O 1-89 [» ]
    2QOY X-ray 3.50 O 1-89 [» ]
    2QP0 X-ray 3.50 O 1-89 [» ]
    2VAZ electron microscopy 10.00 F 2-89 [» ]
    2WWL electron microscopy 5.80 O 2-89 [» ]
    2YKR electron microscopy 9.80 O 2-89 [» ]
    2Z4K X-ray 4.45 O 1-89 [» ]
    2Z4M X-ray 4.45 O 1-89 [» ]
    3DF1 X-ray 3.50 O 1-89 [» ]
    3DF3 X-ray 3.50 O 1-89 [» ]
    3E1A electron microscopy 9.00 H 1-89 [» ]
    3E1C electron microscopy 9.00 H 1-89 [» ]
    3FIH electron microscopy 6.70 O 2-89 [» ]
    3I1M X-ray 3.19 O 1-89 [» ]
    3I1O X-ray 3.19 O 1-89 [» ]
    3I1Q X-ray 3.81 O 1-89 [» ]
    3I1S X-ray 3.81 O 1-89 [» ]
    3I1Z X-ray 3.71 O 1-89 [» ]
    3I21 X-ray 3.71 O 1-89 [» ]
    3IZV electron microscopy - S 1-89 [» ]
    3IZW electron microscopy - S 1-89 [» ]
    3J00 electron microscopy - O 2-89 [» ]
    3J18 electron microscopy 8.30 O 2-89 [» ]
    3J36 electron microscopy 9.80 O 2-89 [» ]
    3J4V electron microscopy 12.00 O 1-89 [» ]
    3J4W electron microscopy 12.00 O 1-89 [» ]
    3J4Y electron microscopy 17.00 O 1-89 [» ]
    3J4Z electron microscopy 20.00 O 1-89 [» ]
    3J53 electron microscopy 13.00 O 1-89 [» ]
    3J55 electron microscopy 15.00 O 1-89 [» ]
    3J57 electron microscopy 17.00 O 1-89 [» ]
    3J59 electron microscopy 12.00 O 1-89 [» ]
    3J5B electron microscopy 17.00 O 1-89 [» ]
    3J5D electron microscopy 17.00 O 1-89 [» ]
    3J5F electron microscopy 20.00 O 1-89 [» ]
    3J5H electron microscopy 15.00 O 1-89 [» ]
    3J5J electron microscopy 9.00 O 1-89 [» ]
    3J5N electron microscopy 6.80 O 1-89 [» ]
    3J5T electron microscopy 7.60 O 2-89 [» ]
    3J5X electron microscopy 7.60 O 2-89 [» ]
    3KC4 electron microscopy - O 1-89 [» ]
    3OAQ X-ray 3.25 O 2-89 [» ]
    3OAR X-ray 3.25 O 2-89 [» ]
    3OFA X-ray 3.19 O 2-89 [» ]
    3OFB X-ray 3.19 O 2-89 [» ]
    3OFO X-ray 3.10 O 2-89 [» ]
    3OFP X-ray 3.10 O 2-89 [» ]
    3OFX X-ray 3.29 O 2-89 [» ]
    3OFY X-ray 3.29 O 2-89 [» ]
    3OR9 X-ray 3.30 O 1-89 [» ]
    3ORA X-ray 3.30 O 1-89 [» ]
    3SFS X-ray 3.20 O 1-89 [» ]
    3UOQ X-ray 3.70 O 1-89 [» ]
    4A2I electron microscopy 16.50 O 2-89 [» ]
    4ADV electron microscopy 13.50 O 1-89 [» ]
    4GAQ X-ray 3.30 O 1-89 [» ]
    4GAS X-ray 3.30 O 1-89 [» ]
    4GD1 X-ray 3.00 O 2-89 [» ]
    4GD2 X-ray 3.00 O 2-89 [» ]
    4KIY X-ray 2.90 O 1-89 [» ]
    4KJ0 X-ray 2.90 O 1-89 [» ]
    4KJ2 X-ray 2.90 O 1-89 [» ]
    4KJ4 X-ray 2.90 O 1-89 [» ]
    4KJ6 X-ray 2.90 O 1-89 [» ]
    4KJ8 X-ray 2.90 O 1-89 [» ]
    4KJA X-ray 2.90 O 1-89 [» ]
    4KJC X-ray 2.90 O 1-89 [» ]
    ProteinModelPortali P0ADZ4.
    SMRi P0ADZ4. Positions 3-88.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-47909N.
    IntActi P0ADZ4. 30 interactions.
    MINTi MINT-1299353.
    STRINGi 511145.b3165.

    Chemistry

    ChEMBLi CHEMBL2363135.

    Proteomic databases

    PaxDbi P0ADZ4.
    PRIDEi P0ADZ4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76199 ; AAC76199 ; b3165 .
    BAE77211 ; BAE77211 ; BAE77211 .
    GeneIDi 12933439.
    947686.
    KEGGi ecj:Y75_p3087.
    eco:b3165.
    PATRICi 32121748. VBIEscCol129921_3260.

    Organism-specific databases

    EchoBASEi EB0907.
    EcoGenei EG10914. rpsO.

    Phylogenomic databases

    eggNOGi COG0184.
    HOGENOMi HOG000040097.
    KOi K02956.
    OMAi NKQDHHS.
    OrthoDBi EOG6B368J.
    PhylomeDBi P0ADZ4.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10914-MONOMER.
    ECOL316407:JW3134-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0ADZ4.
    PROi P0ADZ4.

    Gene expression databases

    Genevestigatori P0ADZ4.

    Family and domain databases

    Gene3Di 1.10.287.10. 1 hit.
    HAMAPi MF_01343_B. Ribosomal_S15_B.
    InterProi IPR000589. Ribosomal_S15.
    IPR005290. Ribosomal_S15_bac-type.
    IPR009068. S15_NS1_RNA-bd.
    [Graphical view ]
    Pfami PF00312. Ribosomal_S15. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47060. SSF47060. 1 hit.
    TIGRFAMsi TIGR00952. S15_bact. 1 hit.
    PROSITEi PS00362. RIBOSOMAL_S15. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the gene for Escherichia coli ribosomal protein S15 (rpsO)."
      Takata R., Mukai T., Aoyagi M., Hori K.
      Mol. Gen. Genet. 197:225-229(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Expression of the rpsO and pnp genes: structural analysis of a DNA fragment carrying their control regions."
      Portier C., Regnier P.
      Nucleic Acids Res. 12:6091-6102(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Promoter activity and transcript mapping in the regulatory region for genes encoding ribosomal protein S15 and polynucleotide phosphorylase of Escherichia coli."
      Evans S., Dennis P.P.
      Gene 40:15-22(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Nucleotide sequence of the pnp gene of Escherichia coli encoding polynucleotide phosphorylase. Homology of the primary structure of the protein with the RNA-binding domain of ribosomal protein S1."
      Regnier P., Grunberg-Manago M., Portier C.
      J. Biol. Chem. 262:63-68(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    6. "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.
    7. "Primary structure of the 16S rRNA binding protein S15 from Escherichia coli ribosomes."
      Morinaga T., Funatsu G., Funatsu M., Wittmann H.G.
      FEBS Lett. 64:307-309(1976) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-89.
      Strain: K.
    8. "The existence of two genes between infB and rpsO in the Escherichia coli genome: DNA sequencing and S1 nuclease mapping."
      Sands J.F., Regnier P., Cummings H.S., Grunberg-Manago M., Hershey J.W.B.
      Nucleic Acids Res. 16:10803-10816(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
    9. "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.
    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), INTERSUBUNIT BRIDGE FORMATION.
      Strain: MRE-600.
    13. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES INCLUDING THE INTERSUBUNIT BRIDGE.
      Strain: MRE-600.

    Entry informationi

    Entry nameiRS15_ECOLI
    AccessioniPrimary (citable) accession number: P0ADZ4
    Secondary accession number(s): P02371, Q2M945
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 88 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