P0A705 (IF2_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 83.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Translation initiation factor IF-2 | ||||||
| Gene names |
| ||||||
| Organism | Escherichia coli (strain K12) [Reference proteome] [HAMAP] | ||||||
| Taxonomic identifier | 83333 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 890 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex. HAMAP-Rule MF_00100_B |
| Subcellular location | |
| 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. HAMAP-Rule MF_00100_B |
| Sequence similarities | Belongs to the IF-2 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm |
| Coding sequence diversity | Alternative initiation |
| Ligand | GTP-binding Nucleotide-binding |
| Molecular function | Initiation factor |
| PTM | Acetylation |
| Technical term | 3D-structure Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell membraneInferred from direct assay PubMed 16858726. Source: UniProtKB |
| Molecular_function | GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activityInferred from direct assay PubMed 4337107. Source: EcoCyc guanosine tetraphosphate bindingInferred from direct assay PubMed 16968770. Source: EcoCyc ribosomal small subunit bindingInferred from direct assay PubMed 16935296. Source: EcoCyc translation initiation factor activityInferred from direct assay PubMed 4872321PubMed 4876939PubMed 4943554. Source: EcoCyc |
| Complete GO annotation... | |
Alternative products
| This entry describes 3 isoforms produced by alternative initiation. [Align] [Select] | ||||||
| Isoform Alpha (identifier: P0A705-1) 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. | ||||||
| Isoform Beta (identifier: P0A705-2) The sequence of this isoform differs from the canonical sequence as follows: 1-157: Missing. 158-158: V → M | ||||||
| Isoform Beta' (identifier: P0A705-3) The sequence of this isoform differs from the canonical sequence as follows: 1-164: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||
Molecule processing | ||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 890 | 890 | Translation initiation factor IF-2 HAMAP-Rule MF_00100_B | PRO_0000238785 | ||||||||||||||
Regions | ||||||||||||||||||
| Nucleotide binding | 398 – 405 | 8 | GTP By similarity | |||||||||||||||
| Nucleotide binding | 444 – 448 | 5 | GTP By similarity | |||||||||||||||
| Nucleotide binding | 498 – 501 | 4 | GTP By similarity | |||||||||||||||
| Region | 1 – 103 | 103 | 1 HAMAP-Rule MF_00100_B | |||||||||||||||
| Region | 104 – 287 | 184 | 2 HAMAP-Rule MF_00100_B | |||||||||||||||
| Region | 288 – 391 | 104 | 3 HAMAP-Rule MF_00100_B | |||||||||||||||
| Region | 392 – 540 | 149 | G-domain HAMAP-Rule MF_00100_B | |||||||||||||||
| Region | 541 – 668 | 128 | 5 HAMAP-Rule MF_00100_B | |||||||||||||||
| Region | 669 – 890 | 222 | 6 HAMAP-Rule MF_00100_B | |||||||||||||||
| Compositional bias | 167 – 214 | 48 | Ala/Arg/Glu/Lys-rich HAMAP-Rule MF_00100_B | |||||||||||||||
Amino acid modifications | ||||||||||||||||||
| Modified residue | 808 | 1 | N6-acetyllysine Ref.12 | |||||||||||||||
Natural variations | ||||||||||||||||||
| Alternative sequence | 1 – 164 | 164 | Missing in isoform Beta'. | VSP_018760 | ||||||||||||||
| Alternative sequence | 1 – 157 | 157 | Missing in isoform Beta. | VSP_018758 | ||||||||||||||
| Alternative sequence | 158 | 1 | V → M in isoform Beta. | VSP_018759 | ||||||||||||||
| Natural variant | 409 | 1 | D → E in strain: IQ489. | |||||||||||||||
| Natural variant | 423 | 1 | G → GG in strain: IQ490. | |||||||||||||||
| Natural variant | 432 | 1 | H → Q in strain: ECOAU9326. | |||||||||||||||
| Natural variant | 490 | 1 | Q → G in strain: ECOAU9302, ECOAU9306, ECOAU9307 and ECOAU9309. | |||||||||||||||
| Natural variant | 684 | 1 | G → A in strain: ECOAU9306. | |||||||||||||||
Secondary structure | ||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||
| Helix | 8 – 13 | 6 | ||||||||||||||||
| Beta strand | 14 – 16 | 3 | ||||||||||||||||
| Helix | 17 – 27 | 11 | ||||||||||||||||
| Beta strand | 32 – 35 | 4 | ||||||||||||||||
| Helix | 41 – 43 | 3 | ||||||||||||||||
| Helix | 44 – 49 | 6 | ||||||||||||||||
Sequences
| ||||||||||||||||||||||||||||||
References
| « Hide 'large scale' references | |
| [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] | "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 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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] | "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. |
| [8] | "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 (ISOFORMS BETA AND BETA'). |
| [9] | "Structural and functional domains of E coli initiation factor IF2." Laalami S., Sacerdot C., Vachon G., Mortensen K., Sperling-Petersen H.U., Cenatiempo Y., Grunberg-Manago M. Biochimie 73:1557-1566(1991) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN STRUCTURE. |
| [10] | "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. |
| [11] | "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. |
| [12] | "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, MASS SPECTROMETRY. Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | 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. | ||||||||||||||||||
| PIR | FIEC2. D65107. | ||||||||||||||||||
| RefSeq | NP_417637.1. NC_000913.2. YP_491355.1. NC_007779.1. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||
| ProteinModelPortal | P0A705. | ||||||||||||||||||
| SMR | P0A705. Positions 2-50, 344-887. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| DIP | DIP-36182N. | ||||||||||||||||||
| IntAct | P0A705. 45 interactions. | ||||||||||||||||||
| MINT | MINT-1235405. | ||||||||||||||||||
PTM databases | |||||||||||||||||||
| PhosSite | P010442. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PRIDE | P0A705. | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| EnsemblBacteria | AAC76202; AAC76202; b3168. BAE77214; BAE77214; BAE77214. | ||||||||||||||||||
| GeneID | 12933442. 947684. | ||||||||||||||||||
| KEGG | ecj:Y75_p3090. eco:b3168. | ||||||||||||||||||
| PATRIC | 32121754. VBIEscCol129921_3263. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| EchoBASE | EB0500. | ||||||||||||||||||
| EcoGene | EG10505. infB. | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| KO | K02519. | ||||||||||||||||||
| OMA | NILGIAE. | ||||||||||||||||||
| ProtClustDB | PRK05306. | ||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||
| BioCyc | EcoCyc:EG10505-MONOMER. ECOL316407:JW3137-MONOMER. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| Genevestigator | P0A705. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| Gene3D | 3.40.50.10050. 1 hit. | ||||||||||||||||||
| HAMAP | MF_00100_B. IF-2_B. | ||||||||||||||||||
| InterPro | IPR009061. DNA-bd_dom_put. IPR000795. EF_GTP-bd_dom. IPR013575. IF2_assoc_dom_bac. IPR006847. IF2_N. IPR005225. Small_GTP-bd_dom. IPR000178. TF_IF2_bacterial-like. IPR015760. TIF_IF2. IPR023115. TIF_IF2_dom3. IPR004161. Transl_elong_EFTu/EF1A_2. IPR009000. Transl_elong_init/rib_B-barrel. [Graphical view] | ||||||||||||||||||
| PANTHER | PTHR23115:SF41. PTHR23115:SF41. 1 hit. | ||||||||||||||||||
| Pfam | PF00009. GTP_EFTU. 1 hit. PF03144. GTP_EFTU_D2. 2 hits. PF11987. IF-2. 1 hit. PF08364. IF2_assoc. 1 hit. PF04760. IF2_N. 2 hits. [Graphical view] | ||||||||||||||||||
| SUPFAM | SSF46955. Putativ_DNA_bind. 1 hit. SSF52156. TIF_IF2_dom3. 1 hit. SSF50447. Translat_factor. 2 hits. | ||||||||||||||||||
| TIGRFAMs | TIGR00487. IF-2. 1 hit. TIGR00231. small_GTP. 1 hit. | ||||||||||||||||||
| PROSITE | PS01176. IF2. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other | |||||||||||||||||||
| EvolutionaryTrace | P0A705. | ||||||||||||||||||
Entry information
| Entry name | IF2_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P0A705 Secondary accession number(s): O32548 Q9EV00 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Translation initiation factors List of translation initiation factor entries |
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
