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P0A707

- IF3_ECOLI

UniProt

P0A707 - IF3_ECOLI

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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

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. ribosome binding Source: EcoCyc
  2. translation initiation factor activity Source: EcoCyc

GO - Biological processi

  1. response to cold Source: EcoCyc
  2. ribosome disassembly Source: EcoCyc
Complete GO annotation...

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-KW
  2. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi107 – 1071Y → F or L: Reduced ribosome binding. 1 Publication
Mutagenesisi110 – 1101K → R or L: Reduced ribosome binding. 1 Publication

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 – 987Combined sources
Helixi104 – 1074Combined sources
Helixi109 – 11911Combined sources
Beta strandi122 – 1287Combined sources
Helixi140 – 15213Combined sources
Turni153 – 1553Combined sources
Beta strandi156 – 1594Combined sources
Beta strandi171 – 1766Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP0A707.
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

        10         20         30         40         50
MKGGKRVQTA RPNRINGEIR AQEVRLTGLE GEQLGIVSLR EALEKAEEAG
60 70 80 90 100
VDLVEISPNA EPPVCRIMDY GKFLYEKSKS SKEQKKKQKV IQVKEIKFRP
110 120 130 140 150
GTDEGDYQVK LRSLIRFLEE GDKAKITLRF RGREMAHQQI GMEVLNRVKD
160 170 180
DLQELAVVES FPTKIEGRQM IMVLAPKKKQ
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P0A707.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 91 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