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Protein

Translation initiation factor IF-2

Gene

infB

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

Functioni

One of the essential components for the initiation of protein synthesis. May protect N-formylmethionyl-tRNA(fMet) from spontaneous hydrolysis. Promotes N-formylmethionyl-tRNA(fMet) binding to the 30S pre-initiation complex (PIC) (PubMed:1764105, PubMed:20224578). Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex. Upon addition of the 50S ribosomal subunit, IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initation complex.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi398 – 4058GTPBy similarity
Nucleotide bindingi444 – 4485GTPBy similarity
Nucleotide bindingi498 – 5014GTPBy similarity

GO - Molecular functioni

  • GTPase activity Source: EcoCyc
  • GTP binding Source: UniProtKB-KW
  • guanosine tetraphosphate binding Source: EcoCyc
  • ribosomal small subunit binding Source: EcoCyc
  • translation initiation factor activity Source: EcoliWiki

GO - Biological processi

  • translational initiation Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10505-MONOMER.
ECOL316407:JW3137-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Translation initiation factor IF-2
Gene namesi
Name:infB
Synonyms:gicD, ssyG
Ordered Locus Names:b3168, JW3137
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10505. infB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Essential, it cannot be deleted. The C-terminal region (residues 165-890) is sufficient for growth at 42 degrees Celsius, although it grows more slowly at 37 degrees and is cold-sensitive at 30 degrees Celsius (PubMed:1374802).1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi158 – 1581V → A: Produces 35% of isoform beta (i.e. only beta2). 1 Publication
Mutagenesisi158 – 1581V → E: Produces 70% of isoform beta (i.e. only beta2). 1 Publication
Mutagenesisi158 – 1581V → G: Produces 66% of isoform beta (i.e. only beta2). 1 Publication
Mutagenesisi165 – 1651M → I or T: Produces reduces amount of isoform beta (i.e. only beta1). Reduced growth at 37 degrees Celsius, greatly reduced growth at 30 degrees Celsius. Growth is more impaired; when associated with silent V-158 GUG to GUC. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 890890Translation initiation factor IF-2PRO_0000238785Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei808 – 8081N6-acetyllysine1 Publication

Post-translational modificationi

A proteolyzed form, called IF2 gamma (begins with residue 290), can be detected during purification which has all the activities expected for this protein, although it is slightly less efficient than full-length protein. It is not clear if it exists in vivo.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP0A705.
PaxDbiP0A705.
PRIDEiP0A705.

PTM databases

iPTMnetiP0A705.

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.3 Publications

Protein-protein interaction databases

DIPiDIP-36182N.
IntActiP0A705. 45 interactions.
MINTiMINT-1235405.
STRINGi511145.b3168.

Structurei

Secondary structure

1
890
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 136Combined sources
Beta strandi14 – 163Combined sources
Helixi17 – 2711Combined sources
Beta strandi32 – 354Combined sources
Helixi41 – 433Combined sources
Helixi44 – 496Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ND9NMR-A2-50[»]
1ZO1electron microscopy13.80I388-888[»]
3JCJelectron microscopy3.70f1-890[»]
3JCNelectron microscopy4.60b1-890[»]
ProteinModelPortaliP0A705.
SMRiP0A705. Positions 2-50, 316-887.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A705.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini389 – 558170tr-type GAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 1031031Add
BLAST
Regioni104 – 2871842Add
BLAST
Regioni288 – 3911043Add
BLAST
Regioni398 – 4058G1By similarity
Regioni423 – 4275G2By similarity
Regioni444 – 4474G3By similarity
Regioni498 – 5014G4By similarity
Regioni534 – 5363G5By similarity
Regioni541 – 6681285Add
BLAST
Regioni669 – 8902226Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi167 – 21448Ala/Arg/Glu/Lys-richAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4107QHU. Bacteria.
COG0532. LUCA.
InParanoidiP0A705.
KOiK02519.
OMAiKFAVVES.
OrthoDBiEOG67HJSV.
PhylomeDBiP0A705.

Family and domain databases

Gene3Di3.40.50.10050. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00100_B. IF_2_B.
InterProiIPR009061. DNA-bd_dom_put.
IPR013575. IF2_assoc_dom_bac.
IPR006847. IF2_N.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR000178. TF_IF2_bacterial-like.
IPR023115. TIF_IF2_dom3.
IPR009000. Transl_B-barrel.
[Graphical view]
PfamiPF11987. IF-2. 1 hit.
PF08364. IF2_assoc. 1 hit.
PF04760. IF2_N. 2 hits.
[Graphical view]
SUPFAMiSSF46955. SSF46955. 1 hit.
SSF50447. SSF50447. 2 hits.
SSF52156. SSF52156. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00487. IF-2. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEiPS51722. G_TR_2. 1 hit.
PS01176. IF2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform Alpha1 Publication (identifier: P0A705-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTDVTIKTLA AERQTSVERL VQQFADAGIR KSADDSVSAQ EKQTLIDHLN
60 70 80 90 100
QKNSGPDKLT LQRKTRSTLN IPGTGGKSKS VQIEVRKKRT FVKRDPQEAE
110 120 130 140 150
RLAAEEQAQR EAEEQARREA EESAKREAQQ KAEREAAEQA KREAAEQAKR
160 170 180 190 200
EAAEKDKVSN QQDDMTKNAQ AEKARREQEA AELKRKAEEE ARRKLEEEAR
210 220 230 240 250
RVAEEARRMA EENKWTDNAE PTEDSSDYHV TTSQHARQAE DESDREVEGG
260 270 280 290 300
RGRGRNAKAA RPKKGNKHAE SKADREEARA AVRGGKGGKR KGSSLQQGFQ
310 320 330 340 350
KPAQAVNRDV VIGETITVGE LANKMAVKGS QVIKAMMKLG AMATINQVID
360 370 380 390 400
QETAQLVAEE MGHKVILRRE NELEEAVMSD RDTGAAAEPR APVVTIMGHV
410 420 430 440 450
DHGKTSLLDY IRSTKVASGE AGGITQHIGA YHVETENGMI TFLDTPGHAA
460 470 480 490 500
FTSMRARGAQ ATDIVVLVVA ADDGVMPQTI EAIQHAKAAQ VPVVVAVNKI
510 520 530 540 550
DKPEADPDRV KNELSQYGIL PEEWGGESQF VHVSAKAGTG IDELLDAILL
560 570 580 590 600
QAEVLELKAV RKGMASGAVI ESFLDKGRGP VATVLVREGT LHKGDIVLCG
610 620 630 640 650
FEYGRVRAMR NELGQEVLEA GPSIPVEILG LSGVPAAGDE VTVVRDEKKA
660 670 680 690 700
REVALYRQGK FREVKLARQQ KSKLENMFAN MTEGEVHEVN IVLKADVQGS
710 720 730 740 750
VEAISDSLLK LSTDEVKVKI IGSGVGGITE TDATLAAASN AILVGFNVRA
760 770 780 790 800
DASARKVIEA ESLDLRYYSV IYNLIDEVKA AMSGMLSPEL KQQIIGLAEV
810 820 830 840 850
RDVFKSPKFG AIAGCMVTEG VVKRHNPIRV LRDNVVIYEG ELESLRRFKD
860 870 880 890
DVNEVRNGME CGIGVKNYND VRTGDVIEVF EIIEIQRTIA
Note: Isoform alpha is approximately 2-fold more abundant than the combined beta isoforms. Optimal growth requires both alpha and beta IF2.1 Publication
Length:890
Mass (Da):97,350
Last modified:June 7, 2005 - v1
Checksum:i86B9F9B2AE773DDE
GO
Isoform Beta3 Publications (identifier: P0A705-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-157: Missing.
     158-158: V → M

Note: Also called beta1.1 Publication
Show »
Length:733
Mass (Da):79,745
Checksum:iA85674E0145D5E66
GO
Isoform Beta'2 Publications (identifier: P0A705-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-164: Missing.

Note: Also called beta2.1 Publication
Show »
Length:726
Mass (Da):78,927
Checksum:i08C16925C01D0199
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti409 – 4091D → E in strain: IQ489.
Natural varianti423 – 4231G → GG in strain: IQ490.
Natural varianti432 – 4321H → Q in strain: ECOAU9326.
Natural varianti490 – 4901Q → G in strain: ECOAU9302, ECOAU9306, ECOAU9307 and ECOAU9309.
Natural varianti684 – 6841G → A in strain: ECOAU9306.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 164164Missing in isoform Beta'. Curated2 PublicationsVSP_018760Add
BLAST
Alternative sequencei1 – 157157Missing in isoform Beta. Curated3 PublicationsVSP_018758Add
BLAST
Alternative sequencei158 – 1581V → M in isoform Beta. 2 PublicationsVSP_018759

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00513 Genomic DNA. Translation: CAA25201.1.
X00513 Genomic DNA. Translation: CAA25202.1.
U18997 Genomic DNA. Translation: AAA57971.1.
U00096 Genomic DNA. Translation: AAC76202.1.
AP009048 Genomic DNA. Translation: BAE77214.1.
AJ002537 Genomic DNA. Translation: CAA05529.1.
AJ002537 Genomic DNA. Translation: CAA05530.1.
AJ002537 Genomic DNA. Translation: CAA05531.1.
AJ002538 Genomic DNA. Translation: CAA05532.1.
AJ002538 Genomic DNA. Translation: CAA05533.1.
AJ002538 Genomic DNA. Translation: CAA05534.1.
AJ002539 Genomic DNA. Translation: CAA05535.1.
AJ002539 Genomic DNA. Translation: CAA05536.1.
AJ002539 Genomic DNA. Translation: CAA05537.1.
AJ002540 Genomic DNA. Translation: CAA05538.1.
AJ002540 Genomic DNA. Translation: CAA05539.1.
AJ002540 Genomic DNA. Translation: CAA05540.1.
AJ002541 Genomic DNA. Translation: CAA05541.1.
AJ002541 Genomic DNA. Translation: CAA05542.1.
AJ002541 Genomic DNA. Translation: CAA05543.1.
AJ002542 Genomic DNA. Translation: CAA05544.1.
AJ002542 Genomic DNA. Translation: CAA05545.1.
AJ002542 Genomic DNA. Translation: CAA05546.1.
AJ002402 Genomic DNA. Translation: CAA05386.1.
AJ002403 Genomic DNA. Translation: CAA05387.1.
AJ002404 Genomic DNA. Translation: CAA05388.1.
AJ002405 Genomic DNA. Translation: CAA05389.1.
AJ002406 Genomic DNA. Translation: CAA05390.1.
AJ002407 Genomic DNA. Translation: CAA05391.1.
AJ002408 Genomic DNA. Translation: CAA05392.1.
AJ002409 Genomic DNA. Translation: CAA05393.1.
AJ002410 Genomic DNA. Translation: CAA05394.1.
AJ002411 Genomic DNA. Translation: CAA05395.1.
AJ002412 Genomic DNA. Translation: CAA05396.1.
AJ002413 Genomic DNA. Translation: CAA05397.1.
AJ132861 Genomic DNA. Translation: CAC20126.1.
AJ132861 Genomic DNA. Translation: CAC20127.1.
AJ132861 Genomic DNA. Translation: CAC20128.1.
AJ132862 Genomic DNA. Translation: CAC20130.1.
AJ132862 Genomic DNA. Translation: CAC20131.1.
AJ132862 Genomic DNA. Translation: CAC20132.1.
X13775 Genomic DNA. Translation: CAA32019.1.
PIRiD65107. FIEC2.
RefSeqiNP_417637.1. NC_000913.3.
WP_000133044.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76202; AAC76202; b3168.
BAE77214; BAE77214; BAE77214.
GeneIDi947684.
KEGGiecj:JW3137.
eco:b3168.
PATRICi32121754. VBIEscCol129921_3263.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00513 Genomic DNA. Translation: CAA25201.1.
X00513 Genomic DNA. Translation: CAA25202.1.
U18997 Genomic DNA. Translation: AAA57971.1.
U00096 Genomic DNA. Translation: AAC76202.1.
AP009048 Genomic DNA. Translation: BAE77214.1.
AJ002537 Genomic DNA. Translation: CAA05529.1.
AJ002537 Genomic DNA. Translation: CAA05530.1.
AJ002537 Genomic DNA. Translation: CAA05531.1.
AJ002538 Genomic DNA. Translation: CAA05532.1.
AJ002538 Genomic DNA. Translation: CAA05533.1.
AJ002538 Genomic DNA. Translation: CAA05534.1.
AJ002539 Genomic DNA. Translation: CAA05535.1.
AJ002539 Genomic DNA. Translation: CAA05536.1.
AJ002539 Genomic DNA. Translation: CAA05537.1.
AJ002540 Genomic DNA. Translation: CAA05538.1.
AJ002540 Genomic DNA. Translation: CAA05539.1.
AJ002540 Genomic DNA. Translation: CAA05540.1.
AJ002541 Genomic DNA. Translation: CAA05541.1.
AJ002541 Genomic DNA. Translation: CAA05542.1.
AJ002541 Genomic DNA. Translation: CAA05543.1.
AJ002542 Genomic DNA. Translation: CAA05544.1.
AJ002542 Genomic DNA. Translation: CAA05545.1.
AJ002542 Genomic DNA. Translation: CAA05546.1.
AJ002402 Genomic DNA. Translation: CAA05386.1.
AJ002403 Genomic DNA. Translation: CAA05387.1.
AJ002404 Genomic DNA. Translation: CAA05388.1.
AJ002405 Genomic DNA. Translation: CAA05389.1.
AJ002406 Genomic DNA. Translation: CAA05390.1.
AJ002407 Genomic DNA. Translation: CAA05391.1.
AJ002408 Genomic DNA. Translation: CAA05392.1.
AJ002409 Genomic DNA. Translation: CAA05393.1.
AJ002410 Genomic DNA. Translation: CAA05394.1.
AJ002411 Genomic DNA. Translation: CAA05395.1.
AJ002412 Genomic DNA. Translation: CAA05396.1.
AJ002413 Genomic DNA. Translation: CAA05397.1.
AJ132861 Genomic DNA. Translation: CAC20126.1.
AJ132861 Genomic DNA. Translation: CAC20127.1.
AJ132861 Genomic DNA. Translation: CAC20128.1.
AJ132862 Genomic DNA. Translation: CAC20130.1.
AJ132862 Genomic DNA. Translation: CAC20131.1.
AJ132862 Genomic DNA. Translation: CAC20132.1.
X13775 Genomic DNA. Translation: CAA32019.1.
PIRiD65107. FIEC2.
RefSeqiNP_417637.1. NC_000913.3.
WP_000133044.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ND9NMR-A2-50[»]
1ZO1electron microscopy13.80I388-888[»]
3JCJelectron microscopy3.70f1-890[»]
3JCNelectron microscopy4.60b1-890[»]
ProteinModelPortaliP0A705.
SMRiP0A705. Positions 2-50, 316-887.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-36182N.
IntActiP0A705. 45 interactions.
MINTiMINT-1235405.
STRINGi511145.b3168.

PTM databases

iPTMnetiP0A705.

Proteomic databases

EPDiP0A705.
PaxDbiP0A705.
PRIDEiP0A705.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76202; AAC76202; b3168.
BAE77214; BAE77214; BAE77214.
GeneIDi947684.
KEGGiecj:JW3137.
eco:b3168.
PATRICi32121754. VBIEscCol129921_3263.

Organism-specific databases

EchoBASEiEB0500.
EcoGeneiEG10505. infB.

Phylogenomic databases

eggNOGiENOG4107QHU. Bacteria.
COG0532. LUCA.
InParanoidiP0A705.
KOiK02519.
OMAiKFAVVES.
OrthoDBiEOG67HJSV.
PhylomeDBiP0A705.

Enzyme and pathway databases

BioCyciEcoCyc:EG10505-MONOMER.
ECOL316407:JW3137-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A705.
PROiP0A705.

Family and domain databases

Gene3Di3.40.50.10050. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00100_B. IF_2_B.
InterProiIPR009061. DNA-bd_dom_put.
IPR013575. IF2_assoc_dom_bac.
IPR006847. IF2_N.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR000178. TF_IF2_bacterial-like.
IPR023115. TIF_IF2_dom3.
IPR009000. Transl_B-barrel.
[Graphical view]
PfamiPF11987. IF-2. 1 hit.
PF08364. IF2_assoc. 1 hit.
PF04760. IF2_N. 2 hits.
[Graphical view]
SUPFAMiSSF46955. SSF46955. 1 hit.
SSF50447. SSF50447. 2 hits.
SSF52156. SSF52156. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00487. IF-2. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEiPS51722. G_TR_2. 1 hit.
PS01176. IF2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of the initiation factor IF2 gene: unusual protein features and homologies with elongation factors."
    Sacerdot C., Dessen P., Hershey J.W.B., Plumbridge J.A., Grunberg-Manago M.
    Proc. Natl. Acad. Sci. U.S.A. 81:7787-7791(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "E. coli translation initiation factor IF2--an extremely conserved protein. Comparative sequence analysis of the infB gene in clinical isolates of E. coli."
    Steffensen S.A.D.A., Poulsen A.B., Mortensen K.K., Sperling-Petersen H.U.
    FEBS Lett. 419:281-284(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Various clinical strains.
  3. "Sequence of the infB gene from Escherichia coli strain IQ489 and IQ490."
    Hedegaard J., Kristensen J.E., Nakamura Y., Sperling-Petersen H.U., Mortensen K.K.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: IQ489 and IQ490.
  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. "The nucleotide sequence of the cloned nusA gene and its flanking region of Escherichia coli."
    Ishii S., Ihara M., Maekawa T., Nakamura Y., Uchida H., Imamoto F.
    Nucleic Acids Res. 12:3333-3342(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
  7. "Two translational initiation sites in the infB gene are used to express initiation factor IF2 alpha and IF2 beta in Escherichia coli."
    Plumbridge J.A., Deville F., Sacerdot C., Petersen H.U., Cenatiempo Y., Cozzone A., Grunberg-Manago M., Hershey J.W.
    EMBO J. 4:223-229(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-11 AND 159-174 (ISOFORMS ALPHA AND BETA).
  8. "The existence of two genes between infB and rpsO in the Escherichia coli genome: DNA sequencing and S1 nuclease mapping."
    Sands J.F., Regnier P., Cummings H.S., Grunberg-Manago M., Hershey J.W.B.
    Nucleic Acids Res. 16:10803-10816(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 864-890.
  9. "Tandem translation of E. coli initiation factor IF2 beta: purification and characterization in vitro of two active forms."
    Nyengaard N.R., Mortensen K.K., Lassen S.F., Hershey J.W.B., Sperling-Petersen H.U.
    Biochem. Biophys. Res. Commun. 181:1572-1579(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 159-174 AND 166-174 (ISOFORMS BETA AND BETA'), FUNCTION, SUBCELLULAR LOCATION.
  10. "Both forms of translational initiation factor IF2 (alpha and beta) are required for maximal growth of Escherichia coli. Evidence for two translational initiation codons for IF2 beta."
    Sacerdot C., Vachon G., Laalami S., Morel-Deville F., Cenatiempo Y., Grunberg-Manago M.
    J. Mol. Biol. 225:67-80(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 159-169 AND 166-171 (ISOFORMS BETA AND BETA'), FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF VAL-158 AND MET-165.
  11. "The protein synthesis initiation factor 2 G-domain. Study of a functionally active C-terminal 65-kilodalton fragment of IF2 from Escherichia coli."
    Cenatiempo Y., Deville F., Dondon J., Grunberg-Manago M., Sacerdot C., Hershey J.W., Hansen H.F., Petersen H.U., Clark B.F., Kjeldgaard M.
    Biochemistry 26:5070-5076(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 290-304, FUNCTION, PROTEOLYTIC CLEAVAGE.
  12. Cited for: DOMAIN STRUCTURE, REVIEW.
  13. "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.
  14. "Genetic interaction screens with ordered overexpression and deletion clone sets implicate the Escherichia coli GTPase YjeQ in late ribosome biogenesis."
    Campbell T.L., Brown E.D.
    J. Bacteriol. 190:2537-2545(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIALLY SUPPRESSES A RSGA MUTANT.
    Strain: K12.
  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-808, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  16. "The ribosome-bound initiation factor 2 recruits initiator tRNA to the 30S initiation complex."
    Milon P., Carotti M., Konevega A.L., Wintermeyer W., Rodnina M.V., Gualerzi C.O.
    EMBO Rep. 11:312-316(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  17. "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.
  18. "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.
  19. "A conserved structural motif at the N terminus of bacterial translation initiation factor IF2."
    Laursen B.S., Mortensen K.K., Sperling-Petersen H.U., Hoffman D.W.
    J. Biol. Chem. 278:16320-16328(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 2-50.
    Strain: K12.
  20. "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 nameiIF2_ECOLI
AccessioniPrimary (citable) accession number: P0A705
Secondary accession number(s): O32548
, O32549, O32550, O34379, O34415, O34603, P02995, Q2M942, Q9EUZ4, Q9EUZ5, Q9EUZ6, Q9EUZ8, Q9EUZ9, Q9EV00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 7, 2005
Last modified: May 11, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

When overexpressed partially suppresses the slow growth and decreased 70S ribosome phenotype of an rsgA knockout; RsgA may be involved in 30S ribosomal subunit biogenesis.1 Publication
Silent mutations of codon 158, which no longer function as alternative start codons, decrease beta isoform expression to 31 to 50%, the strongest mutation is GUG to GUC.1 Publication

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

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.