Reviewed,
UniProtKB/Swiss-Prot P0A705 (IF2_ECOLI)
Last modified
June 16, 2009.
Version 47.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Translation initiation factor IF-2 | ||||||
| Gene names |
| ||||||
| Organism | Escherichia coli (strain K12) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 83333 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 890 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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 MF_00100 |
| 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 MF_00100 |
| 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 |
| Gene Ontology (GO) | |
| Biological process | translational initiation Inferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell membraneInferred from direct assay. Source: UniProtKB |
| Molecular function | GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activityInferred from electronic annotation. Source: HAMAP translation initiation factor activityInferred from electronic annotation. Source: HAMAP |
| 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 MF_00100 | 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 MF_00100 | |||||||||||||||
| Region | 104 – 287 | 184 | 2 HAMAP MF_00100 | |||||||||||||||
| Region | 288 – 391 | 104 | 3 HAMAP MF_00100 | |||||||||||||||
| Region | 392 – 540 | 149 | G-domain HAMAP MF_00100 | |||||||||||||||
| Region | 541 – 668 | 128 | 5 HAMAP MF_00100 | |||||||||||||||
| Region | 669 – 890 | 222 | 6 HAMAP MF_00100 | |||||||||||||||
| Compositional bias | 167 – 214 | 48 | Ala/Arg/Glu/Lys-rich HAMAP MF_00100 | |||||||||||||||
Amino acid modifications | ||||||||||||||||||
| Modified residue | 808 | 1 | N6-acetyllysine Ref.11 | |||||||||||||||
Natural variations | ||||||||||||||||||
| Alternative sequence | 1 – 164 | 164 | Missing in isoform Beta'. HAMAP MF_00100 | VSP_018760 | ||||||||||||||
| Alternative sequence | 1 – 157 | 157 | Missing in isoform Beta. HAMAP MF_00100 | VSP_018758 | ||||||||||||||
| Alternative sequence | 158 | 1 | V → M in isoform Beta. HAMAP MF_00100 | VSP_018759 | ||||||||||||||
| Natural variant | 409 | 1 | D → E in strain: IQ489. HAMAP MF_00100 | |||||||||||||||
| Natural variant | 423 | 1 | G → GG in strain: IQ490. HAMAP MF_00100 | |||||||||||||||
| Natural variant | 432 | 1 | H → Q in strain: ECOAU9326. HAMAP MF_00100 | |||||||||||||||
| Natural variant | 490 | 1 | Q → G in strain: ECOAU9302, ECOAU9306, ECOAU9307 and ECOAU9309. HAMAP MF_00100 | |||||||||||||||
| Natural variant | 684 | 1 | G → A in strain: ECOAU9306. HAMAP MF_00100 | |||||||||||||||
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
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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: 6096856] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | Steffensen S.A.D.A., Poulsen A.B., Hedegaard J., Fage-Larsen J., Palacios-Moreno J.M., Andersen L.D., Korsager B., Mortensen K.K., Sperling-Petersen H.U. Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases 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: 9278503] [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: 16738553] [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: 6326058] [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: 2849753] [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: 1764105] [Abstract] Cited for: PROTEIN SEQUENCE OF 159-174 (ISOFORMS BETA-2 AND BETA-2'). |
| [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: 1805969] [Abstract] Cited for: DOMAIN STRUCTURE. |
| [10] | "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: 18223068] [Abstract] Cited for: PARTIALLY SUPPRESSES A RSGA MUTANT. Strain: K12. |
| [11] | "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: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-808, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 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 | AP_003713.1. NP_417637.1. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| |||||||||||||||||||
| SMR | P0A705. Positions 388-888. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
PTM databases | |||||||||||||||||||
| PhosSite | P0A705. | ||||||||||||||||||
2-D gel databases | |||||||||||||||||||
| ECO2DBASE | F119.0. 6TH EDITION. G117.0. 6TH EDITION. | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| GeneID | 947684. | ||||||||||||||||||
| GenomeReviews | Gene locus JW3137 in contig AP009048_GR. Gene locus b3168 in contig U00096_GR. | ||||||||||||||||||
| KEGG | ecj:JW3137. eco:b3168. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| EchoBASE | EB0500. | ||||||||||||||||||
| EcoGene | EG10505. infB. | ||||||||||||||||||
| CMR | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| OMA | P0A705. RGMVTFL. | ||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||
| BioCyc | EcoCyc:EG10505-MON. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| HAMAP | MF_00100. [Tree] | ||||||||||||||||||
| InterPro | IPR015760. aIF-2. IPR000178. IF2. IPR013575. IF2_assoc_bac. IPR006847. IF2_N. IPR000795. ProtSyn_GTP_bd. IPR005225. Small_GTP_bd. IPR004161. Transl_elong_EFTu/EF1A_2. [Graphical view] | ||||||||||||||||||
| PANTHER | PTHR23115:SF41. aIF-2. 1 hit. | ||||||||||||||||||
| Pfam | PF00009. GTP_EFTU. 1 hit. PF03144. GTP_EFTU_D2. 2 hits. PF08364. IF2_assoc. 1 hit. PF04760. IF2_N. 2 hits. [Graphical view] | ||||||||||||||||||
| TIGRFAMs | TIGR00487. IF-2. 1 hit. TIGR00231. small_GTP. 1 hit. | ||||||||||||||||||
| PROSITE | PS01176. IF2. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
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 project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| Translation initiation factors List of translation initiation factor entries |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


