A4J108 (EFG_DESRM) 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:	Dred_0212

Organism

Desulfotomaculum reducens (strain MI-1) [Complete proteome] [HAMAP]

Taxonomic identifier

349161 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Peptococcaceae › Desulfotomaculum

Protein attributes

Sequence length	692 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 – 692	692	Elongation factor G HAMAP MF_00054_B		PRO_1000071144
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)
	A4J108 [UniParc]. Last modified May 1, 2007. Version 1. Checksum: ADA748253BF808DC	FASTA	692	76,379
	10 20 30 40 50 60 MARQFPLERT RNIGIMAHID AGKTTTTERI LFYTGRVHKI GEVHDGAATM DWMVQEQERG 70 80 90 100 110 120 ITITSAATTA QWNGHRVNII DTPGHVDFTV EVERSLRVLD GAVAVFCSVG GVEPQSETVW 130 140 150 160 170 180 RQADKYGVPR LAYINKMDRV GADFFNGMDM IKNRLGANPV AIQLPIGSED RFKGIVDLVT 190 200 210 220 230 240 KKAIVYIDDL GTNSETTDIP ADMVDQVEEY REKLLEAVAE SDEELMMKYL EGEELTEEEI 250 260 270 280 290 300 KVAIRKATLA VKITPVICGS SFKNKGVQSL LDAIVDYLPA PTDVPPIQGV NPDTGTEDQR 310 320 330 340 350 360 ISSDNEPFAA LAFKIMTDPY VGKLSYFRVY SGTLKSGSYV LNSTKGKKER VGRILQMHAN 370 380 390 400 410 420 HREEIPEVYA GDIAAAVGLK DTTTGDTLCD EKSLIILESM EFPDPVIHVA IEPKTKADQD 430 440 450 460 470 480 KMGVALSKLS EEDPTFKVRT DEETGQTIIA GMGELHLEII VDRLLREFKV QANVGRPQVA 490 500 510 520 530 540 YKETIRKAVK AEGKFVRQSG GKGQYGHVWI ELEPLEAGGP GYEFVNKIVG GVVPREYIAP 550 560 570 580 590 600 VDNGIKEAME NGILAGYQMV DIKATLYDGS YHEVDSSEMA FKIAGSMAFK NGAQKANPVL 610 620 630 640 650 660 LEPIFKVEVT VPEEYMGDVI GDLNSRRGRI EEMGQRGNAR IVSAFVPLAE MFGYATDLRS 670 680 690 KTQGRGTYSM QHDHYEEVPK NIAEGIIAKR KG

References

[1]

"Complete sequence of Desulfotomaculum reducens MI-1." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. , Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P. Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MI-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000612 Genomic DNA. Translation: ABO48761.1.
RefSeq	YP_001111586.1. NC_009253.1.
3D structure databases
ProteinModelPortal	A4J108.
SMR	A4J108. Positions 4-687.
ModBase	Search...
Protein-protein interaction databases
STRING	A4J108.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4957332.
GenomeReviews	Gene locus Dred_0212 in contig CP000612_GR.
KEGG	drm:Dred_0212.
PATRIC	21726224. VBIDesRed82656_0221.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0480.
HOGENOM	HBG737692.
OMA	CNEWREK.
PhylomeDB	A4J108.
ProtClustDB	PRK00007.
Enzyme and pathway databases
BioCyc	DRED349161:DRED_0212-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_DESRM

Accession

Primary (citable) accession number: A4J108

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	May 1, 2007
Last modified:	January 25, 2012
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program