Q8KTB2 (EFG_RICTY) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 70.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Elongation factor G Short name=EF-G | ||||
| Gene names |
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| Organism | Rickettsia typhi (strain ATCC VR-144 / Wilmington) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 257363 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › typhus group › ![]() |
Protein attributes
| Sequence length | 699 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome By similarity. HAMAP-Rule MF_00054 |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the GTP-binding elongation factor family. EF-G/EF-2 subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | GTP-binding Nucleotide-binding |
| Molecular function | Elongation factor |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | GTP catabolic process Inferred from electronic annotation. Source: GOC |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | GTP binding Inferred from electronic annotation. Source: HAMAP GTPase activityInferred from electronic annotation. Source: InterPro translation elongation factor activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 699 | 699 | Elongation factor G HAMAP-Rule MF_00054 | PRO_0000091205 | |||||
Regions | |||||||||
| Nucleotide binding | 17 – 24 | 8 | GTP By similarity | ||||||
| Nucleotide binding | 81 – 85 | 5 | GTP By similarity | ||||||
| Nucleotide binding | 135 – 138 | 4 | GTP By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 263 | 1 | F → L in AAM90925. Ref.1 | ||||||
| Sequence conflict | 306 | 1 | T → L in AAM90925. Ref.1 | ||||||
| Sequence conflict | 641 | 1 | S → K in AAM90925. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Proliferation and deterioration of Rickettsia palindromic elements." Amiri H., Alsmark C.M., Andersson S.G.E. Mol. Biol. Evol. 19:1234-1243(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Complete genome sequence of Rickettsia typhi and comparison with sequences of other Rickettsiae." McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A. Weinstock G.M.J. Bacteriol. 186:5842-5855(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC VR-144 / Wilmington. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF502176 Genomic DNA. Translation: AAM90925.1. AE017197 Genomic DNA. Translation: AAU03607.1. |
| RefSeq | YP_067089.1. NC_006142.1. |
3D structure databases | |
| ProteinModelPortal | Q8KTB2. |
| SMR | Q8KTB2. Positions 5-694. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 257363.RT0121. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAU03607; AAU03607; RT0121. |
| GeneID | 2958765. |
| KEGG | rty:RT0121. |
| PATRIC | 17909414. VBIRicTyp34752_0128. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0480. |
| HOGENOM | HOG000231585. |
| KO | K02355. |
| OMA | QEPGKGY. |
| ProtClustDB | PRK12739. |
Enzyme and pathway databases | |
| BioCyc | RTYP257363:GJEQ-129-MONOMER. |
Family and domain databases | |
| Gene3D | 3.30.230.10. 1 hit. 3.30.70.240. 1 hit. |
| HAMAP | MF_00054_B. EF-G_EF-2_B. |
| InterPro | IPR000795. EF_GTP-bd_dom. IPR009022. EFG_III-V. IPR000640. EFG_V. IPR020568. Ribosomal_S5_D2-typ_fold. IPR014721. Ribosomal_S5_D2-typ_fold_subgr. IPR005225. Small_GTP-bd_dom. IPR004540. Transl_elong_EFG/EF2. IPR005517. Transl_elong_EFG/EF2_IV. IPR004161. Transl_elong_EFTu/EF1A_2. IPR009000. Transl_elong_init/rib_B-barrel. [Graphical view] |
| Pfam | PF00679. EFG_C. 1 hit. PF03764. EFG_IV. 1 hit. PF00009. GTP_EFTU. 1 hit. PF03144. GTP_EFTU_D2. 1 hit. [Graphical view] |
| PRINTS | PR00315. ELONGATNFCT. |
| SMART | SM00838. EFG_C. 1 hit. SM00889. EFG_IV. 1 hit. [Graphical view] |
| SUPFAM | SSF54980. EFG_III_V. 2 hits. SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit. SSF50447. Translat_factor. 1 hit. |
| TIGRFAMs | TIGR00484. EF-G. 1 hit. TIGR00231. small_GTP. 1 hit. |
| PROSITE | PS00301. EFACTOR_GTP. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | EFG_RICTY | ||||||||
| Accession | Primary (citable) accession number: Q8KTB2 Secondary accession number(s): Q68XN5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Rickettsia typhi Rickettsia typhi (strain Wilmington): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with
