Q8K9Q9 (LEPA_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Elongation factor 4
Short name=EF-4
EC=3.6.5.n1

Alternative name(s):
Ribosomal back-translocase LepA

Gene names

Name:	lepA
Ordered Locus Names:	BUsg_251

Organism

Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]

Taxonomic identifier

198804 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Schizaphis graminum)

Protein attributes

Sequence length	601 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner By similarity. HAMAP-Rule MF_00071
Catalytic activity	GTP + H2O = GDP + phosphate. HAMAP-Rule MF_00071
Subcellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity HAMAP-Rule MF_00071.
Sequence similarities	Belongs to the GTP-binding elongation factor family. LepA subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cell membrane Membrane
Ligand	GTP-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	GTP catabolic process Inferred from electronic annotation. Source: GOC positive regulation of translation Inferred from electronic annotation. Source: HAMAP translational elongation Inferred from electronic annotation. Source: GOC
Cellular_component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	GTP binding Inferred from electronic annotation. Source: HAMAP GTPase activity Inferred from electronic annotation. Source: HAMAP ribosome binding Inferred from electronic annotation. Source: HAMAP translation elongation factor activity Inferred 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 – 601	601	Elongation factor 4 HAMAP-Rule MF_00071		PRO_0000176247
Regions
	Nucleotide binding	18 – 23	6	GTP By similarity
	Nucleotide binding	135 – 138	4	GTP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8K9Q9 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: AAEA8B0EF6091ECA	FASTA	601	67,748
	10 20 30 40 50 60 MVKKMKNIRN FSIIAHIDHG KSTLSDRLIQ KCGGLSEREM SDQVLDSMDL EKERGITIKA 70 80 90 100 110 120 QSVMIDYKDK NGNVFHLNFI DTPGHVNFSY EVSRSLAACE GALLVVDSSQ GVEAQTLANC 130 140 150 160 170 180 ATALEMKLSI VPVLNKIDLP NSNPEKVARE IKEIIGISAL DAIRCSAKTG QGIEELIEQI 190 200 210 220 230 240 IKKIPAPDGD EKKPLQALII DSWFDNYLGV VSLIRIKNGI ISKKDKIKVM STGKTYFVDH 250 260 270 280 290 300 LGIFTPKKIN KNYLKCGEVG WIVCGIKNIS AAPVGDTLTN AKNPAMNMLT GFKKIKPQIY 310 320 330 340 350 360 AGLFPVTSDQ YEIFRDALGK LSLNDSSLFY EPINSTALGF GFRCGFLGLL HMEIVQARLE 370 380 390 400 410 420 REYSLNLIST APNVIYQIEF NNGEKIYLDT PSNFPVDNKI RKIKEPIVEC NILLPPKFLG 430 440 450 460 470 480 PVMKLCIKKR GTEINMIYHE QQVSLKYHIP MNEVVLNFFD ELKSVSSGYA SLEYDFKYFK 490 500 510 520 530 540 TVKMVRIDIL INSERVDALT VISYYKNAQN RAREIVNKMK ELIPRHQFDI NIQATINNSI 550 560 570 580 590 600 VARSTIKQLR KNVLAKCYGG DISRKKKLLK KQKDGKKRMK KIGNVNMPKT AFLDILNIHK D

References

[1]

"50 million years of genomic stasis in endosymbiotic bacteria." Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E. Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sg.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE013218 Genomic DNA. Translation: AAM67810.1.
RefSeq	NP_660599.1. NC_004061.1.
3D structure databases
ProteinModelPortal	Q8K9Q9.
SMR	Q8K9Q9. Positions 5-559.
ModBase	Search...
Protein-protein interaction databases
STRING	198804.BUsg251.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM67810; AAM67810; BUsg_251.
GeneID	1005453.
KEGG	bas:BUsg251.
PATRIC	21247305. VBIBucAph100086_0262.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0481.
KO	K03596.
OMA	KCYGGDA.
ProtClustDB	PRK05433.
Enzyme and pathway databases
BioCyc	BAPH198804:GHMG-312-MONOMER.
Family and domain databases
Gene3D	3.30.70.240. 1 hit.
HAMAP	MF_00071. LepA.
InterPro	IPR006297. EF-4. IPR000795. EF_GTP-bd_dom. IPR009022. EFG_III-V. IPR000640. EFG_V. IPR013842. LepA_GTP-bd_C. IPR005225. Small_GTP-bd_dom. IPR004161. Transl_elong_EFTu/EF1A_2. IPR009000. Transl_elong_init/rib_B-barrel. [Graphical view]
PANTHER	PTHR23115:SF40. PTHR23115:SF40. 1 hit.
Pfam	PF00679. EFG_C. 1 hit. PF00009. GTP_EFTU. 1 hit. PF03144. GTP_EFTU_D2. 1 hit. PF06421. LepA_C. 1 hit. [Graphical view]
PRINTS	PR00315. ELONGATNFCT.
SMART	SM00838. EFG_C. 1 hit. [Graphical view]
SUPFAM	SSF54980. EFG_III_V. 2 hits. SSF50447. Translat_factor. 1 hit.
TIGRFAMs	TIGR01393. lepA. 1 hit. TIGR00231. small_GTP. 1 hit.
PROSITE	PS00301. EFACTOR_GTP. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LEPA_BUCAP

Accession

Primary (citable) accession number: Q8K9Q9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2002
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program