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P0A707 (IF3_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Translation initiation factor IF-3
Gene names
Name:infC
Synonyms:fit
Ordered Locus Names:b1718, JW5829
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length180 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_00080

Subunit structure

Monomer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00080.

Post-translational modification

Phosphorylated on threonine residue(s). Ref.8

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.

Sequence similarities

Belongs to the IF-3 family.

Caution

Was originally (Ref.10) 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 (Ref.12).

Binary interactions

With

Entry

#Exp.

IntAct

Notes

rpsGP023593EBI-546262,EBI-543074

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 180180Translation initiation factor IF-3 HAMAP-Rule MF_00080
PRO_0000367498
Initiator methionine11Removed; alternate HAMAP-Rule MF_00080
Chain2 – 180179Translation initiation factor IF-3, N-terminally processed HAMAP-Rule MF_00080
PRO_0000014499
Chain7 – 180174Translation initiation factor IF-3S HAMAP-Rule MF_00080
PRO_0000364089

Sites

Site1071Important for 30S binding
Site1101Important for 30S binding

Amino acid modifications

Modified residue11N-methylmethionine; in Translation initiation factor IF-3; alternate Ref.1

Experimental info

Mutagenesis1071Y → F or L: Reduced ribosome binding. Ref.9
Mutagenesis1101K → R or L: Reduced ribosome binding. Ref.9
Sequence conflict221Q → E AA sequence Ref.1
Sequence conflict34 – 363LGI → IGMV AA sequence Ref.1
Sequence conflict471E → Q AA sequence Ref.1
Sequence conflict521D → N AA sequence Ref.1
Sequence conflict611E → Q AA sequence Ref.1
Sequence conflict871K → E AA sequence Ref.1
Sequence conflict901V → K AA sequence Ref.1
Sequence conflict1031D → N AA sequence Ref.1
Sequence conflict1051G → N AA sequence Ref.1
Sequence conflict1611F → S in AAA51467. Ref.3
Sequence conflict1781K → Q AA sequence Ref.1
Sequence conflict1801Missing AA sequence Ref.1

Secondary structure

............... 180
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A707 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 6120EB6AD42E9ABE

FASTA18020,564
        10         20         30         40         50         60 
MKGGKRVQTA RPNRINGEIR AQEVRLTGLE GEQLGIVSLR EALEKAEEAG VDLVEISPNA 

        70         80         90        100        110        120 
EPPVCRIMDY GKFLYEKSKS SKEQKKKQKV IQVKEIKFRP GTDEGDYQVK LRSLIRFLEE 

       130        140        150        160        170        180 
GDKAKITLRF RGREMAHQQI GMEVLNRVKD DLQELAVVES FPTKIEGRQM IMVLAPKKKQ 

« Hide

References

« Hide 'large scale' references
[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]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00291 Genomic DNA. Translation: CAA23561.1.
K02844 Genomic DNA. Translation: AAA51467.1.
U00096 Genomic DNA. Translation: AAC74788.1.
AP009048 Genomic DNA. Translation: BAA15485.1.
PIRFIEC3. S13748.
RefSeqNP_416233.1. NC_000913.3.
YP_489980.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IFENMR-A81-180[»]
DisProtDP00197.
ProteinModelPortalP0A707.
SMRP0A707. Positions 15-86, 90-180.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-36176N.
IntActP0A707. 48 interactions.
MINTMINT-1221578.
STRING511145.b1718.

Chemistry

ChEMBLCHEMBL1075077.

PTM databases

PhosSiteP010443.

Proteomic databases

PaxDbP0A707.
PRIDEP0A707.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74788; AAC74788; b1718.
BAA15485; BAA15485; BAA15485.
GeneID12933198.
946225.
KEGGecj:Y75_p1693.
eco:b1718.
PATRIC32118740. VBIEscCol129921_1788.

Organism-specific databases

EchoBASEEB0501.
EcoGeneEG10506. infC.

Phylogenomic databases

eggNOGCOG0290.
HOGENOMHOG000035157.
KOK02520.
OMARQMMMVI.
OrthoDBEOG63JRGJ.
PhylomeDBP0A707.

Enzyme and pathway databases

BioCycEcoCyc:EG10506-MONOMER.
ECOL316407:JW5829-MONOMER.

Gene expression databases

GenevestigatorP0A707.

Family and domain databases

Gene3D3.10.20.80. 1 hit.
3.30.110.10. 1 hit.
HAMAPMF_00080. IF_3.
InterProIPR019813. Translation_initiation_fac3_CS.
IPR001288. Translation_initiation_fac_3.
IPR019815. Translation_initiation_fac_3_C.
IPR019814. Translation_initiation_fac_3_N.
[Graphical view]
PANTHERPTHR10938. PTHR10938. 1 hit.
PfamPF00707. IF3_C. 1 hit.
PF05198. IF3_N. 1 hit.
[Graphical view]
SUPFAMSSF54364. SSF54364. 1 hit.
SSF55200. SSF55200. 1 hit.
TIGRFAMsTIGR00168. infC. 1 hit.
PROSITEPS00938. IF3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A707.
PROP0A707.

Entry information

Entry nameIF3_ECOLI
AccessionPrimary (citable) accession number: P0A707
Secondary accession number(s): P02999, P76905
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Translation initiation factors

List of translation initiation factor entries

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene