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)

P0AD49

- RAIA_ECOLI

UniProt

P0AD49 - RAIA_ECOLI

Protein

Ribosome-associated inhibitor A

Gene

raiA

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

    During stationary phase, prevents 70S dimer formation, probably in order to regulate translation efficiency during transition between the exponential and the stationary phases. In addition, during environmental stress such as cold shock or excessive cell density at stationary phase, stabilizes the 70S ribosome against dissociation, inhibits translation initiation and increase translation accuracy. When normal growth conditions are restored, is quickly released from the ribosome. Inhibits translation initiation by blocking the A-site (aminoacyl-tRNA site) and P-site (peptidyl-tRNA site) of the ribosome. Counteracts miscoding (translation errors) particularly efficiently at magnesium concentrations close to those observed in vivo but less efficiently at higher concentrations. Counteraction of miscoding was shown to be stronger than inhibition of translation, suggesting that the former activity could be the main function of RaiA in vivo.6 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. ribosomal small subunit binding Source: EcoCyc

    GO - Biological processi

    1. negative regulation of translational elongation Source: EcoCyc
    2. negative regulation of translational initiation Source: EcoCyc
    3. primary metabolic process Source: InterPro
    4. response to cold Source: EcoCyc

    Keywords - Biological processi

    Stress response, Translation regulation

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11151-MONOMER.
    ECOL316407:JW2578-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribosome-associated inhibitor A
    Alternative name(s):
    Protein Y
    SpotY
    Short name:
    pY
    Gene namesi
    Name:raiA
    Synonyms:yfiA
    Ordered Locus Names:b2597, JW2578
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11151. raiA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosolic small ribosomal subunit Source: EcoliWiki

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 113112Ribosome-associated inhibitor APRO_0000169261Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei66 – 661N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP0AD49.
    PRIDEiP0AD49.

    2D gel databases

    SWISS-2DPAGEP0AD49.

    Expressioni

    Inductioni

    By environmental stress or during stationary phase.2 Publications

    Gene expression databases

    GenevestigatoriP0AD49.

    Interactioni

    Subunit structurei

    Associates mainly with 70S ribosomes. Localized at the surface of the 30S ribosomal subunit, at the interface with the 50S subunit. Binds across the channel in the 30S subunit where tRNAs and mRNA interact during protein biosynthesis. Can also associate with 100S ribosomes.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    frrP0A8054EBI-1129692,EBI-1114349

    Protein-protein interaction databases

    DIPiDIP-36014N.
    IntActiP0AD49. 7 interactions.
    MINTiMINT-1260187.
    STRINGi511145.b2597.

    Structurei

    Secondary structure

    1
    113
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 85
    Helixi14 – 2310
    Helixi24 – 307
    Beta strandi35 – 428
    Beta strandi48 – 569
    Beta strandi59 – 6911
    Helixi70 – 9021
    Helixi91 – 933
    Helixi98 – 1014
    Beta strandi109 – 1113

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1L4SNMR-A2-113[»]
    1N3GNMR-A1-113[»]
    1VOQX-ray11.50a2-91[»]
    1VOSX-ray11.50a2-91[»]
    1VOVX-ray11.50a2-91[»]
    1VOXX-ray11.50a2-91[»]
    1VOZX-ray11.50a2-91[»]
    3V2CX-ray2.70Y1-113[»]
    3V2EX-ray2.70Y1-113[»]
    ProteinModelPortaliP0AD49.
    SMRiP0AD49. Positions 1-113.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AD49.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni23 – 264Interaction with rRNASequence Analysis
    Regioni83 – 919Interaction with rRNASequence Analysis

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1544.
    HOGENOMiHOG000264774.
    KOiK05809.
    OMAiINITSKQ.
    OrthoDBiEOG618R0J.
    PhylomeDBiP0AD49.

    Family and domain databases

    Gene3Di3.30.160.100. 1 hit.
    InterProiIPR003489. Ribosomal_S30Ae/sigma54_mod.
    [Graphical view]
    PfamiPF02482. Ribosomal_S30AE. 1 hit.
    [Graphical view]
    SUPFAMiSSF69754. SSF69754. 1 hit.
    TIGRFAMsiTIGR00741. yfiA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P0AD49-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTMNITSKQM EITPAIRQHV ADRLAKLEKW QTHLINPHII LSKEPQGFVA    50
    DATINTPNGV LVASGKHEDM YTAINELINK LERQLNKLQH KGEARRAATS 100
    VKDANFVEEV EEE 113
    Length:113
    Mass (Da):12,785
    Last modified:January 23, 2007 - v2
    Checksum:i562901F819836A87
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M10431 Genomic DNA. Translation: AAA24328.1.
    Z70523 Genomic DNA. Translation: CAA94436.1.
    U00096 Genomic DNA. Translation: AAC75646.1.
    AP009048 Genomic DNA. Translation: BAA16481.1.
    M58024 Genomic DNA. Translation: AAA62782.1.
    PIRiA30275. Q5ECPA.
    RefSeqiNP_417088.1. NC_000913.3.
    YP_490820.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75646; AAC75646; b2597.
    BAA16481; BAA16481; BAA16481.
    GeneIDi12932624.
    947129.
    KEGGiecj:Y75_p2545.
    eco:b2597.
    PATRICi32120595. VBIEscCol129921_2696.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M10431 Genomic DNA. Translation: AAA24328.1 .
    Z70523 Genomic DNA. Translation: CAA94436.1 .
    U00096 Genomic DNA. Translation: AAC75646.1 .
    AP009048 Genomic DNA. Translation: BAA16481.1 .
    M58024 Genomic DNA. Translation: AAA62782.1 .
    PIRi A30275. Q5ECPA.
    RefSeqi NP_417088.1. NC_000913.3.
    YP_490820.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1L4S NMR - A 2-113 [» ]
    1N3G NMR - A 1-113 [» ]
    1VOQ X-ray 11.50 a 2-91 [» ]
    1VOS X-ray 11.50 a 2-91 [» ]
    1VOV X-ray 11.50 a 2-91 [» ]
    1VOX X-ray 11.50 a 2-91 [» ]
    1VOZ X-ray 11.50 a 2-91 [» ]
    3V2C X-ray 2.70 Y 1-113 [» ]
    3V2E X-ray 2.70 Y 1-113 [» ]
    ProteinModelPortali P0AD49.
    SMRi P0AD49. Positions 1-113.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-36014N.
    IntActi P0AD49. 7 interactions.
    MINTi MINT-1260187.
    STRINGi 511145.b2597.

    2D gel databases

    SWISS-2DPAGE P0AD49.

    Proteomic databases

    PaxDbi P0AD49.
    PRIDEi P0AD49.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75646 ; AAC75646 ; b2597 .
    BAA16481 ; BAA16481 ; BAA16481 .
    GeneIDi 12932624.
    947129.
    KEGGi ecj:Y75_p2545.
    eco:b2597.
    PATRICi 32120595. VBIEscCol129921_2696.

    Organism-specific databases

    EchoBASEi EB1140.
    EcoGenei EG11151. raiA.

    Phylogenomic databases

    eggNOGi COG1544.
    HOGENOMi HOG000264774.
    KOi K05809.
    OMAi INITSKQ.
    OrthoDBi EOG618R0J.
    PhylomeDBi P0AD49.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG11151-MONOMER.
    ECOL316407:JW2578-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0AD49.
    PROi P0AD49.

    Gene expression databases

    Genevestigatori P0AD49.

    Family and domain databases

    Gene3Di 3.30.160.100. 1 hit.
    InterProi IPR003489. Ribosomal_S30Ae/sigma54_mod.
    [Graphical view ]
    Pfami PF02482. Ribosomal_S30AE. 1 hit.
    [Graphical view ]
    SUPFAMi SSF69754. SSF69754. 1 hit.
    TIGRFAMsi TIGR00741. yfiA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence and transcription of the phenylalanine and tyrosine operons of Escherichia coli K12."
      Hudson G.S., Davidson B.E.
      J. Mol. Biol. 180:1023-1051(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Identification of two Escherichia coli K12 proteins which are induced in response to pollutant stress."
      Faber F., van Giezen M., van Gorcom R.F.M., Harder W.
      Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    3. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
      Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
      , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
      DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    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. "pheAo mutants of Escherichia coli have a defective pheA attenuator."
      Gavini N., Davidson B.E.
      J. Biol. Chem. 265:21532-21535(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-113.
    7. "A protein residing at the subunit interface of the bacterial ribosome."
      Agafonov D.E., Kolb V.A., Nazimov I.V., Spirin A.S.
      Proc. Natl. Acad. Sci. U.S.A. 96:12345-12349(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-18, FUNCTION IN STABILIZATION OF THE RIBOSOME, INTERACTION WITH THE RIBOSOMAL 30S SUBUNIT.
      Strain: MRE-600.
    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. "Two proteins, YfiA and YhbH, associated with resting ribosomes in stationary phase Escherichia coli."
      Maki Y., Yoshida H., Wada A.
      Genes Cells 5:965-974(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-13, FUNCTION, INTERACTION WITH 70S AND 100S RIBOSOMES, INDUCTION.
    10. Cited for: PROTEIN SEQUENCE OF 2-12.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    11. "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography."
      Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.
      Electrophoresis 20:2181-2195(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: B / BL21.
    12. "Ribosome-associated protein that inhibits translation at the aminoacyl-tRNA binding stage."
      Agafonov D.E., Kolb V.A., Spirin A.S.
      EMBO Rep. 2:399-402(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN BLOCKING OF THE RIBOSOMAL A-SITE, FUNCTION IN INHIBITION OF TRANSLATION, INDUCTION, GENE NAME.
      Strain: MRE-600.
    13. "The ribosome-associated inhibitor A reduces translation errors."
      Agafonov D.E., Spirin A.S.
      Biochem. Biophys. Res. Commun. 320:354-358(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN THE REDUCTION OF TRANSLATION ERRORS.
    14. "Ribosome binding proteins YhbH and YfiA have opposite functions during 100S formation in the stationary phase of Escherichia coli."
      Ueta M., Yoshida H., Wada C., Baba T., Mori H., Wada A.
      Genes Cells 10:1103-1112(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN THE PREVENTION OF THE 70S RIBOSOME DIMERIZATION.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    15. "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-66, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
    16. "Solution structure of the ribosome-associated cold shock response protein Yfia of Escherichia coli."
      Rak A., Kalinin A., Shcherbakov D., Bayer P.
      Biochem. Biophys. Res. Commun. 299:710-714(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    17. "Ribosome-associated factor Y adopts a fold resembling a double-stranded RNA binding domain scaffold."
      Ye K., Serganov A., Hu W., Garber M., Patel D.J.
      Eur. J. Biochem. 269:5182-5191(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 2-113.
    18. "Structural basis for the control of translation initiation during stress."
      Vila-Sanjurjo A., Schuwirth B.S., Hau C.W., Cate J.H.
      Nat. Struct. Mol. Biol. 11:1054-1059(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (11.50 ANGSTROMS) OF 2-91, FUNCTION IN INHIBITION OF TRANSLATION, BLOCKING OF A- AND P-SITES.
      Strain: MRE-600.

    Entry informationi

    Entry nameiRAIA_ECOLI
    AccessioniPrimary (citable) accession number: P0AD49
    Secondary accession number(s): P11285
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 22, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 79 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    During stress, ribosome stabilization by RaiA could serve to protect from degradation the interface between the ribosomal subunits, the key residues lining the A- and P-sites in the small subunit and possibly and the 3' end of the 16S rRNA.

    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3