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Protein

Translation initiation factor IF-1

Gene

infA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

One of the essential components for the initiation of protein synthesis. Binds in the vicinity of the A-site. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit, IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initation complex.2 Publications

GO - Molecular functioni

  • ribosome binding Source: EcoCyc
  • rRNA binding Source: UniProtKB-HAMAP
  • translation initiation factor activity Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10504-MONOMER.
ECOL316407:JW0867-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Translation initiation factor IF-1UniRule annotation
Gene namesi
Name:infAUniRule annotation
Ordered Locus Names:b0884, JW0867
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10504. infA.

Subcellular locationi

  • Cytoplasm UniRule annotation1 Publication

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 7271Translation initiation factor IF-1PRO_0000095785Add
BLAST

Proteomic databases

EPDiP69222.
PaxDbiP69222.
PRIDEiP69222.

Interactioni

Subunit structurei

Component of the 30S ribosomal translation pre-initiation complex which assembles on the 30S ribosome in the order IF-2 and IF-3, IF-1 and N-formylmethionyl-tRNA(fMet); mRNA recruitment can occur at any time during PIC assembly.UniRule annotation2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
mqsAQ468642EBI-1120746,EBI-1120353

Protein-protein interaction databases

BioGridi4262047. 10 interactions.
DIPiDIP-48250N.
IntActiP69222. 10 interactions.
STRINGi511145.b0884.

Structurei

Secondary structure

1
72
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 166Combined sources
Beta strandi18 – 269Combined sources
Beta strandi31 – 366Combined sources
Helixi40 – 423Combined sources
Beta strandi64 – 674Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AH9NMR-A2-72[»]
1ZO1electron microscopy13.80W34-61[»]
ProteinModelPortaliP69222.
SMRiP69222. Positions 2-72.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP69222.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7271S1-likeUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the IF-1 family.UniRule annotation
Contains 1 S1-like domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG0361. LUCA.
HOGENOMiHOG000221323.
InParanoidiP69222.
KOiK02518.
OMAiKGRIIWR.
OrthoDBiEOG6384SC.
PhylomeDBiP69222.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_00075. IF_1.
InterProiIPR012340. NA-bd_OB-fold.
IPR006196. RNA-binding_domain_S1_IF1.
IPR022967. S1_dom.
IPR004368. TIF_IF1.
[Graphical view]
PfamiPF01176. eIF-1a. 1 hit.
[Graphical view]
SMARTiSM00316. S1. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00008. infA. 1 hit.
PROSITEiPS50832. S1_IF1_TYPE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P69222-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKEDNIEMQ GTVLETLPNT MFRVELENGH VVTAHISGKM RKNYIRILTG
60 70
DKVTVELTPY DLSKGRIVFR SR
Length:72
Mass (Da):8,250
Last modified:January 23, 2007 - v2
Checksum:iCDFE0845C4CBE147
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00373 Genomic DNA. Translation: CAA68446.1.
M63145 Genomic DNA. Translation: AAC36912.1. Sequence problems.
L10383 Unassigned DNA. Translation: AAA03232.1.
U00096 Genomic DNA. Translation: AAC73970.1.
AP009048 Genomic DNA. Translation: BAA35602.1.
PIRiA27855. FIEC1.
RefSeqiNP_415404.1. NC_000913.3.
WP_001040187.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73970; AAC73970; b0884.
BAA35602; BAA35602; BAA35602.
GeneIDi5552070.
945500.
KEGGiecj:JW0867.
eco:b0884.
PATRICi32116977. VBIEscCol129921_0913.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00373 Genomic DNA. Translation: CAA68446.1.
M63145 Genomic DNA. Translation: AAC36912.1. Sequence problems.
L10383 Unassigned DNA. Translation: AAA03232.1.
U00096 Genomic DNA. Translation: AAC73970.1.
AP009048 Genomic DNA. Translation: BAA35602.1.
PIRiA27855. FIEC1.
RefSeqiNP_415404.1. NC_000913.3.
WP_001040187.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AH9NMR-A2-72[»]
1ZO1electron microscopy13.80W34-61[»]
ProteinModelPortaliP69222.
SMRiP69222. Positions 2-72.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262047. 10 interactions.
DIPiDIP-48250N.
IntActiP69222. 10 interactions.
STRINGi511145.b0884.

Proteomic databases

EPDiP69222.
PaxDbiP69222.
PRIDEiP69222.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73970; AAC73970; b0884.
BAA35602; BAA35602; BAA35602.
GeneIDi5552070.
945500.
KEGGiecj:JW0867.
eco:b0884.
PATRICi32116977. VBIEscCol129921_0913.

Organism-specific databases

EchoBASEiEB0499.
EcoGeneiEG10504. infA.

Phylogenomic databases

eggNOGiCOG0361. LUCA.
HOGENOMiHOG000221323.
InParanoidiP69222.
KOiK02518.
OMAiKGRIIWR.
OrthoDBiEOG6384SC.
PhylomeDBiP69222.

Enzyme and pathway databases

BioCyciEcoCyc:EG10504-MONOMER.
ECOL316407:JW0867-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP69222.
PROiP69222.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_00075. IF_1.
InterProiIPR012340. NA-bd_OB-fold.
IPR006196. RNA-binding_domain_S1_IF1.
IPR022967. S1_dom.
IPR004368. TIF_IF1.
[Graphical view]
PfamiPF01176. eIF-1a. 1 hit.
[Graphical view]
SMARTiSM00316. S1. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00008. infA. 1 hit.
PROSITEiPS50832. S1_IF1_TYPE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and mapping of infA, the gene for protein synthesis initiation factor IF1."
    Sands J.F., Cummings H.S., Sacerdot C., Dondon L., Grunberg-Manago M., Hershey J.W.B.
    Nucleic Acids Res. 15:5157-5168(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Structure and expression of the infA operon encoding translational initiation factor IF1. Transcriptional control by growth rate."
    Cummings H.S., Sands J.F., Foreman P.C., Fraser J., Hershey J.W.B.
    J. Biol. Chem. 266:16491-16498(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The N-end rule in Escherichia coli: cloning and analysis of the leucyl, phenylalanyl-tRNA-protein transferase gene aat."
    Shrader T.E., Tobias J.W., Varshavsky A.
    J. Bacteriol. 175:4364-4374(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.
  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. "Structure-function relationships in Escherichia coli initiation factors. II. Elucidation of the primary structure of initiation factor IF-1."
    Pon C.L., Wittmann-Liebold B., Gualerzi C.
    FEBS Lett. 101:157-160(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-72, FUNCTION, SUBCELLULAR LOCATION.
    Strain: MRE-600.
  8. "Small genes/gene-products in Escherichia coli K-12."
    Wasinger V.C., Humphery-Smith I.
    FEMS Microbiol. Lett. 169:375-382(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-11.
    Strain: K12.
  9. "Real-time assembly landscape of bacterial 30S translation initiation complex."
    Milon P., Maracci C., Filonava L., Gualerzi C.O., Rodnina M.V.
    Nat. Struct. Mol. Biol. 19:609-615(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  10. "Kinetic control of translation initiation in bacteria."
    Milon P., Rodnina M.V.
    Crit. Rev. Biochem. Mol. Biol. 47:334-348(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  11. "The structure of the translational initiation factor IF1 from E.coli contains an oligomer-binding motif."
    Sette M., van Tilborg P., Spurio R., Kaptein R., Paci M., Gualerzi C.O., Boelens R.
    EMBO J. 16:1436-1443(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  12. "The cryo-EM structure of a complete 30S translation initiation complex from Escherichia coli."
    Julian P., Milon P., Agirrezabala X., Lasso G., Gil D., Rodnina M.V., Valle M.
    PLoS Biol. 9:E1001095-E1001095(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: MODEL BY ELECTRON MICROSCOPY (18.3 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiIF1_ECOLI
AccessioniPrimary (citable) accession number: P69222
Secondary accession number(s): P02998
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 103 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. 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.