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P0A707

- IF3_ECOLI

UniProt

P0A707 - IF3_ECOLI

Protein

Translation initiation factor IF-3

Gene

infC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei107 – 1071Important for 30S binding
    Sitei110 – 1101Important for 30S binding

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. ribosome binding Source: EcoCyc
    3. translation initiation factor activity Source: EcoCyc

    GO - Biological processi

    1. response to cold Source: EcoCyc
    2. ribosome disassembly Source: EcoCyc

    Keywords - Molecular functioni

    Initiation factor

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10506-MONOMER.
    ECOL316407:JW5829-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Translation initiation factor IF-3UniRule annotation
    Cleaved into the following 2 chains:
    Translation initiation factor IF-3, N-terminally processedUniRule annotation
    Translation initiation factor IF-3SUniRule annotation
    Gene namesi
    Name:infCUniRule annotation
    Synonyms:fit
    Ordered Locus Names:b1718, JW5829
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10506. infC.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi107 – 1071Y → F or L: Reduced ribosome binding. 2 Publications
    Mutagenesisi110 – 1101K → R or L: Reduced ribosome binding. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 180180Translation initiation factor IF-3PRO_0000367498Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate
    Chaini2 – 180179Translation initiation factor IF-3, N-terminally processedPRO_0000014499Add
    BLAST
    Chaini7 – 180174Translation initiation factor IF-3SPRO_0000364089Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-methylmethionine; in Translation initiation factor IF-3; alternate1 Publication

    Post-translational modificationi

    Phosphorylated on threonine residue(s).1 Publication

    Keywords - PTMi

    Cleavage on pair of basic residues, Methylation, Phosphoprotein

    Proteomic databases

    PaxDbiP0A707.
    PRIDEiP0A707.

    PTM databases

    PhosSiteiP010443.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A707.

    Interactioni

    Subunit structurei

    Monomer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    rpsGP023593EBI-546262,EBI-543074

    Protein-protein interaction databases

    DIPiDIP-36176N.
    IntActiP0A707. 48 interactions.
    MINTiMINT-1221578.
    STRINGi511145.b1718.

    Structurei

    Secondary structure

    1
    180
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi92 – 987
    Helixi104 – 1074
    Helixi109 – 11911
    Beta strandi122 – 1287
    Helixi140 – 15213
    Turni153 – 1553
    Beta strandi156 – 1594
    Beta strandi171 – 1766

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2IFENMR-A81-180[»]
    DisProtiDP00197.
    ProteinModelPortaliP0A707.
    SMRiP0A707. Positions 15-86, 90-180.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A707.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the IF-3 family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0290.
    HOGENOMiHOG000035157.
    KOiK02520.
    OMAiRQMMMVI.
    OrthoDBiEOG63JRGJ.
    PhylomeDBiP0A707.

    Family and domain databases

    Gene3Di3.10.20.80. 1 hit.
    3.30.110.10. 1 hit.
    HAMAPiMF_00080. IF_3.
    InterProiIPR019813. Translation_initiation_fac3_CS.
    IPR001288. Translation_initiation_fac_3.
    IPR019815. Translation_initiation_fac_3_C.
    IPR019814. Translation_initiation_fac_3_N.
    [Graphical view]
    PANTHERiPTHR10938. PTHR10938. 1 hit.
    PfamiPF00707. IF3_C. 1 hit.
    PF05198. IF3_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF54364. SSF54364. 1 hit.
    SSF55200. SSF55200. 1 hit.
    TIGRFAMsiTIGR00168. infC. 1 hit.
    PROSITEiPS00938. IF3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0A707-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKGGKRVQTA RPNRINGEIR AQEVRLTGLE GEQLGIVSLR EALEKAEEAG    50
    VDLVEISPNA EPPVCRIMDY GKFLYEKSKS SKEQKKKQKV IQVKEIKFRP 100
    GTDEGDYQVK LRSLIRFLEE GDKAKITLRF RGREMAHQQI GMEVLNRVKD 150
    DLQELAVVES FPTKIEGRQM IMVLAPKKKQ 180
    Length:180
    Mass (Da):20,564
    Last modified:July 21, 1986 - v1
    Checksum:i6120EB6AD42E9ABE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221Q → E AA sequence (PubMed:330233)Curated
    Sequence conflicti34 – 363LGI → IGMV AA sequence (PubMed:330233)Curated
    Sequence conflicti47 – 471E → Q AA sequence (PubMed:330233)Curated
    Sequence conflicti52 – 521D → N AA sequence (PubMed:330233)Curated
    Sequence conflicti61 – 611E → Q AA sequence (PubMed:330233)Curated
    Sequence conflicti87 – 871K → E AA sequence (PubMed:330233)Curated
    Sequence conflicti90 – 901V → K AA sequence (PubMed:330233)Curated
    Sequence conflicti103 – 1031D → N AA sequence (PubMed:330233)Curated
    Sequence conflicti105 – 1051G → N AA sequence (PubMed:330233)Curated
    Sequence conflicti161 – 1611F → S in AAA51467. 1 PublicationCurated
    Sequence conflicti178 – 1781K → Q AA sequence (PubMed:330233)Curated
    Sequence conflicti180 – 1801Missing AA sequence (PubMed:330233)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00291 Genomic DNA. Translation: CAA23561.1.
    K02844 Genomic DNA. Translation: AAA51467.1.
    U00096 Genomic DNA. Translation: AAC74788.1.
    AP009048 Genomic DNA. Translation: BAA15485.1.
    PIRiS13748. FIEC3.
    RefSeqiNP_416233.1. NC_000913.3.
    YP_489980.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74788; AAC74788; b1718.
    BAA15485; BAA15485; BAA15485.
    GeneIDi12933198.
    946225.
    KEGGiecj:Y75_p1693.
    eco:b1718.
    PATRICi32118740. VBIEscCol129921_1788.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00291 Genomic DNA. Translation: CAA23561.1 .
    K02844 Genomic DNA. Translation: AAA51467.1 .
    U00096 Genomic DNA. Translation: AAC74788.1 .
    AP009048 Genomic DNA. Translation: BAA15485.1 .
    PIRi S13748. FIEC3.
    RefSeqi NP_416233.1. NC_000913.3.
    YP_489980.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2IFE NMR - A 81-180 [» ]
    DisProti DP00197.
    ProteinModelPortali P0A707.
    SMRi P0A707. Positions 15-86, 90-180.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-36176N.
    IntActi P0A707. 48 interactions.
    MINTi MINT-1221578.
    STRINGi 511145.b1718.

    Chemistry

    ChEMBLi CHEMBL1075077.

    PTM databases

    PhosSitei P010443.

    Proteomic databases

    PaxDbi P0A707.
    PRIDEi P0A707.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74788 ; AAC74788 ; b1718 .
    BAA15485 ; BAA15485 ; BAA15485 .
    GeneIDi 12933198.
    946225.
    KEGGi ecj:Y75_p1693.
    eco:b1718.
    PATRICi 32118740. VBIEscCol129921_1788.

    Organism-specific databases

    EchoBASEi EB0501.
    EcoGenei EG10506. infC.

    Phylogenomic databases

    eggNOGi COG0290.
    HOGENOMi HOG000035157.
    KOi K02520.
    OMAi RQMMMVI.
    OrthoDBi EOG63JRGJ.
    PhylomeDBi P0A707.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10506-MONOMER.
    ECOL316407:JW5829-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A707.
    PROi P0A707.

    Gene expression databases

    Genevestigatori P0A707.

    Family and domain databases

    Gene3Di 3.10.20.80. 1 hit.
    3.30.110.10. 1 hit.
    HAMAPi MF_00080. IF_3.
    InterProi IPR019813. Translation_initiation_fac3_CS.
    IPR001288. Translation_initiation_fac_3.
    IPR019815. Translation_initiation_fac_3_C.
    IPR019814. Translation_initiation_fac_3_N.
    [Graphical view ]
    PANTHERi PTHR10938. PTHR10938. 1 hit.
    Pfami PF00707. IF3_C. 1 hit.
    PF05198. IF3_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54364. SSF54364. 1 hit.
    SSF55200. SSF55200. 1 hit.
    TIGRFAMsi TIGR00168. infC. 1 hit.
    PROSITEi PS00938. IF3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The primary structure of the initiation factor IF-3 from Escherichia coli."
      Brauer D., Wittmann-Liebold B.
      FEBS Lett. 79:269-275(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, DIFFERENT PROTEIN FORMS, METHYLATION AT MET-1.
      Strain: K.
    2. "Sequence of a 1.26-kb DNA fragment containing the structural gene for E.coli initiation factor IF3: presence of an AUU initiator codon."
      Sacerdot C., Fayat G., Dessen P., Springer M., Plumbridge J.A., Grunberg-Manago M., Blanquet S.
      EMBO J. 1:311-315(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Miller H.I.
      Submitted (NOV-1986) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    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. "Separation of two forms of IF-3 in Escherichia coli by two-dimensional gel electrophoresis."
      Suryanarayana T., Subramanian A.R.
      FEBS Lett. 79:264-268(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: DIFFERENT PROTEIN FORMS.
      Strain: Al9, CP78, K and MRE600.
    8. "Phosphorylation of Escherichia coli translation initiation factors by the bacteriophage T7 protein kinase."
      Robertson E.S., Nicholson A.W.
      Biochemistry 31:4822-4827(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    9. "Structure-function analysis of Escherichia coli translation initiation factor IF3: tyrosine 107 and lysine 110 are required for ribosome binding."
      Debellis D., Liveris D., Goss D., Ringquist S., Schwartz I.
      Biochemistry 31:11984-11990(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-107 AND LYS-110.
    10. "AUU-to-AUG mutation in the initiator codon of the translation initiation factor IF3 abolishes translational autocontrol of its own gene (infC) in vivo."
      Butler J.S., Springer M., Grunberg-Manago M.
      Proc. Natl. Acad. Sci. U.S.A. 84:4022-4025(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: MECHANISM OF TRANSLATION REGULATION.
    11. "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.
    12. "How initiation factors maximize the accuracy of tRNA selection in initiation of bacterial protein synthesis."
      Antoun A., Pavlov M.Y., Lovmar M., Ehrenberg M.
      Mol. Cell 23:183-193(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: MECHANISM OF TRANSLATION REGULATION.
    13. "Site-directed mutagenesis and NMR spectroscopic approaches to the elucidation of the structure-function relationships in translation initiation factors IF1 and IF3."
      Spurio R., Paci M., Pawlik R.T., la Teana A., Digiacco B.V., Pon C.L., Gualerzi C.O.
      Biochimie 73:1001-1006(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR, MUTAGENESIS.
    14. "1H and 15N resonance assignments and structure of the N-terminal domain of Escherichia coli initiation factor 3."
      Garcia C., Fortier P.-L., Blanquet S., Lallemand J.-Y., Dardel F.
      Eur. J. Biochem. 228:395-402(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    15. "Heteronuclear NMR studies of E. coli translation initiation factor IF3. Evidence that the inter-domain region is disordered in solution."
      Moreau M., de Cock E., Fortier P.-L., Garcia C., Albaret C., Blanquet S., Lallemand J.-Y., Dardel F.
      J. Mol. Biol. 266:15-22(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    16. "On the global architecture of initiation factor IF3: a comparative study of the linker regions from the Escherichia coli protein and the Bacillus stearothermophilus protein."
      Hua Y., Raleigh D.P.
      J. Mol. Biol. 278:871-878(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    17. de Cock E., Blanquet S., Lallemand J.-Y., Dardel F.
      Submitted (DEC-1998) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 90-180.

    Entry informationi

    Entry nameiIF3_ECOLI
    AccessioniPrimary (citable) accession number: P0A707
    Secondary accession number(s): P02999, P76905
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 89 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    A short form called IF-3S/IF-3 beta is found both in vivo and in vitro and is probably produced by degradation of the long form IF-3L/IF-3 alpha.

    Caution

    Was originally (PubMed:2954162) thought to control the translation of its own gene by binding to its mRNA; it now seems that discrimination against the AUU start codon is a kinetic effect (PubMed:16857585).2 Publications

    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. Translation initiation factors
      List of translation initiation factor entries
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3