Q3YSU3 (EFG_EHRCJ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Elongation factor G
Short name=EF-G

Gene names

Name:	fusA
Ordered Locus Names:	Ecaj_0161

Organism

Ehrlichia canis (strain Jake) [Complete proteome] [HAMAP]

Taxonomic identifier

269484 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Ehrlichia

Protein attributes

Sequence length	690 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 MF_00054_B
Subcellular location	Cytoplasm By similarity HAMAP MF_00054_B.
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)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro translation elongation factor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 690	690	Elongation factor G HAMAP MF_00054_B		PRO_0000225211
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

Sequences

	Sequence		Length	Mass (Da)
	Q3YSU3 [UniParc]. Last modified September 27, 2005. Version 1. Checksum: D1331B1D9CDBD424	FASTA	690	76,169
	10 20 30 40 50 60 MNIDNELSKC RNIGIMAHID AGKTTTTERI LFYTGKQNRI GEVHEGAASM DWMEQEKERG 70 80 90 100 110 120 ITITSAATTC FWNGHRINII DTPGHVDFTI EVERSLRVLD GAVAVFDGVA GVEPQSETVW 130 140 150 160 170 180 RQADKYNVPR ICFMNKMDRM GADFYRCVDM LVDRLGATPL VLQLPIGSEK DFVGVVDLLE 190 200 210 220 230 240 MRSIIWDEDS LGASFHYGEI PKDMIDKAQE YRNKLLESAV ELNDEAMNLY FEGKEISVSL 250 260 270 280 290 300 LKSCIRTGVI QSKFVPVLCG SAFKNRGVQP LLDAVVDFLP APNDIPVIEA LDVKTSNTIN 310 320 330 340 350 360 VKTSAGGKFV ALAFKVMTDK FVGSLTFIRI YSGKLSSKTT VLNAVKDSTE SIGRILLMHA 370 380 390 400 410 420 NNREDITEAQ AGDIVALAGL KKTVTGDTLC ALDYPVILER MEFPEPVMEI AVEPKSTADQ 430 440 450 460 470 480 EKMGIALSRL VAEDPSLGMY VNPESGQTIL KGMGELHLEV IVDRMRREFN VEANIGAPQV 490 500 510 520 530 540 AYRETITKSV EIEYIHKKQT GGAGQFAKVN ILFEPLPPGS GFQFESKITG GAIPKEYIPG 550 560 570 580 590 600 VQSGLENIRG SGMLAGFPVI DFKATLFDGA FHEVDSSPLA FELAAKGAFR DMVNKAGAIL 610 620 630 640 650 660 LEPIMKVEII TPDEYMGDVI GDINSRRGRV AEMQDRHNTK VILAFIPLAK MFGYVKDLRS 670 680 690 MSQGRAQYSM YFSCYEQVPD NIVANEIKTK

References

[1]

"The genome of the obligately intracellular bacterium Ehrlichia canis reveals themes of complex membrane structure and immune evasion strategies." Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P., Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M., Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C. J. Bacteriol. 188:4015-4023(2006) [PubMed: 16707693] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Jake.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000107 Genomic DNA. Translation: AAZ68212.1.
RefSeq	YP_302810.1. NC_007354.1.
3D structure databases
ProteinModelPortal	Q3YSU3.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3YSU3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3617742.
GenomeReviews	Gene locus Ecaj_0161 in contig CP000107_GR.
KEGG	ecn:Ecaj_0161.
PATRIC	20573810. VBIEhrCan118076_0177.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0480.
HOGENOM	HBG737692.
OMA	CNEWREK.
PhylomeDB	Q3YSU3.
ProtClustDB	PRK00007.
Enzyme and pathway databases
BioCyc	ECAN269484:ECAJ_0161-MONOMER.
Family and domain databases
HAMAP	MF_00054_B. EF-G_EF-2_B. [Tree]
InterPro	IPR009022. Elongation_fac_G/III/V. IPR000795. ProtSyn_GTP-bd. IPR020568. Ribosomal_S5_D2-typ_fold. IPR014721. Ribosomal_S5_D2-typ_fold_subgr. IPR005225. Small_GTP-bd_dom. IPR004540. Transl_elong_EFG/EF2. IPR000640. Transl_elong_EFG/EF2_C. IPR005517. Transl_elong_EFG/EF2_IV. IPR004161. Transl_elong_EFTu/EF1A_2. IPR009000. Transl_elong_init/rib_B-barrel. [Graphical view]
Gene3D	G3DSA:3.30.230.10. Ribosomal_S5_D2-type_fold. 1 hit. G3DSA:3.30.70.240. Transl_elong_EFG/EF2_C. 1 hit.
KO	K02355.
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_EHRCJ

Accession

Primary (citable) accession number: Q3YSU3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	September 27, 2005
Last modified:	January 25, 2012
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program