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Protein

Elongation factor G

Gene

fusA

Organism
Staphylococcus aureus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi17 – 24GTPBy similarity8
Nucleotide bindingi81 – 85GTPBy similarity5
Nucleotide bindingi135 – 138GTPBy similarity4

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor G
Short name:
EF-G
Alternative name(s):
85 kDa vitronectin-binding protein
Gene namesi
Name:fusA
Synonyms:fus
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000912192 – 693Elongation factor GAdd BLAST692

Interactioni

Subunit structurei

Has vitronectin-binding activity.

Protein-protein interaction databases

STRINGi93062.SACOL0593.

Structurei

Secondary structure

1693
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 9Combined sources3
Beta strandi10 – 16Combined sources7
Helixi19 – 21Combined sources3
Helixi23 – 34Combined sources12
Helixi47 – 50Combined sources4
Turni51 – 53Combined sources3
Beta strandi66 – 72Combined sources7
Beta strandi75 – 80Combined sources6
Helixi90 – 98Combined sources9
Beta strandi100 – 107Combined sources8
Turni108 – 110Combined sources3
Helixi114 – 125Combined sources12
Beta strandi130 – 135Combined sources6
Helixi144 – 155Combined sources12
Beta strandi159 – 166Combined sources8
Helixi169 – 171Combined sources3
Beta strandi174 – 177Combined sources4
Turni178 – 181Combined sources4
Beta strandi182 – 185Combined sources4
Beta strandi188 – 191Combined sources4
Beta strandi195 – 197Combined sources3
Helixi201 – 203Combined sources3
Helixi204 – 219Combined sources16
Helixi223 – 230Combined sources8
Helixi237 – 249Combined sources13
Beta strandi254 – 258Combined sources5
Turni261 – 264Combined sources4
Helixi267 – 277Combined sources11
Helixi281 – 283Combined sources3
Beta strandi287 – 291Combined sources5
Beta strandi294 – 301Combined sources8
Beta strandi305 – 307Combined sources3
Beta strandi310 – 319Combined sources10
Turni320 – 322Combined sources3
Beta strandi323 – 336Combined sources14
Beta strandi339 – 343Combined sources5
Turni344 – 347Combined sources4
Beta strandi348 – 352Combined sources5
Beta strandi355 – 358Combined sources4
Beta strandi363 – 365Combined sources3
Beta strandi367 – 370Combined sources4
Beta strandi374 – 379Combined sources6
Beta strandi388 – 391Combined sources4
Beta strandi407 – 416Combined sources10
Helixi417 – 433Combined sources17
Beta strandi438 – 440Combined sources3
Beta strandi448 – 454Combined sources7
Helixi455 – 468Combined sources14
Beta strandi473 – 475Combined sources3
Beta strandi483 – 488Combined sources6
Beta strandi490 – 498Combined sources9
Beta strandi505 – 515Combined sources11
Beta strandi523 – 526Combined sources4
Beta strandi530 – 533Combined sources4
Helixi535 – 537Combined sources3
Helixi538 – 550Combined sources13
Beta strandi553 – 556Combined sources4
Beta strandi561 – 570Combined sources10
Turni573 – 575Combined sources3
Helixi578 – 593Combined sources16
Beta strandi598 – 612Combined sources15
Helixi613 – 615Combined sources3
Helixi616 – 625Combined sources10
Beta strandi629 – 636Combined sources8
Beta strandi639 – 647Combined sources9
Helixi648 – 650Combined sources3
Helixi654 – 661Combined sources8
Turni662 – 664Combined sources3
Beta strandi667 – 677Combined sources11
Helixi680 – 690Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XEXX-ray1.90A/B1-693[»]
3ZZ0X-ray2.80A/B1-693[»]
3ZZTX-ray2.95A/B1-693[»]
3ZZUX-ray2.98A/B1-693[»]
ProteinModelPortaliP68790.
SMRiP68790.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68790.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini8 – 282tr-type GAdd BLAST275

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CEJ. Bacteria.
COG0480. LUCA.

Family and domain databases

CDDicd01434. EFG_mtEFG1_IV. 1 hit.
Gene3Di3.30.230.10. 1 hit.
3.30.70.240. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00054_B. EF_G_EF_2_B. 1 hit.
InterProiIPR009022. EFG_III-V.
IPR000640. EFG_V.
IPR004161. EFTu-like_2.
IPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR004540. Transl_elong_EFG/EF2.
IPR005517. Transl_elong_EFG/EF2_IV.
[Graphical view]
PfamiPF00679. EFG_C. 1 hit.
PF14492. EFG_II. 1 hit.
PF03764. EFG_IV. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SMARTiSM00838. EFG_C. 1 hit.
SM00889. EFG_IV. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF54980. SSF54980. 2 hits.
TIGRFAMsiTIGR00484. EF-G. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P68790-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAREFSLEKT RNIGIMAHID AGKTTTTERI LYYTGRIHKI GETHEGASQM
60 70 80 90 100
DWMEQEQDRG ITITSAATTA AWEGHRVNII DTPGHVDFTV EVERSLRVLD
110 120 130 140 150
GAVTVLDAQS GVEPQTETVW RQATTYGVPR IVFVNKMDKL GANFEYSVST
160 170 180 190 200
LHDRLQANAA PIQLPIGAED EFEAIIDLVE MKCFKYTNDL GTEIEEIEIP
210 220 230 240 250
EDHLDRAEEA RASLIEAVAE TSDELMEKYL GDEEISVSEL KEAIRQATTN
260 270 280 290 300
VEFYPVLCGT AFKNKGVQLM LDAVIDYLPS PLDVKPIIGH RASNPEEEVI
310 320 330 340 350
AKADDSAEFA ALAFKVMTDP YVGKLTFFRV YSGTMTSGSY VKNSTKGKRE
360 370 380 390 400
RVGRLLQMHA NSRQEIDTVY SGDIAAAVGL KDTGTGDTLC GEKNDIILES
410 420 430 440 450
MEFPEPVIHL SVEPKSKADQ DKMTQALVKL QEEDPTFHAH TDEETGQVII
460 470 480 490 500
GGMGELHLDI LVDRMKKEFN VECNVGAPMV SYRETFKSSA QVQGKFSRQS
510 520 530 540 550
GGRGQYGDVH IEFTPNETGA GFEFENAIVG GVVPREYIPS VEAGLKDAME
560 570 580 590 600
NGVLAGYPLI DVKAKLYDGS YHDVDSSEMA FKIAASLALK EAAKKCDPVI
610 620 630 640 650
LEPMMKVTIE MPEEYMGDIM GDVTSRRGRV DGMEPRGNAQ VVNAYVPLSE
660 670 680 690
MFGYATSLRS NTQGRGTYTM YFDHYAEVPK SIAEDIIKKN KGE
Length:693
Mass (Da):76,612
Last modified:January 23, 2007 - v2
Checksum:iBAE273E3A33EEED9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti4E → Q AA sequence (Ref. 2) Curated1
Sequence conflicti8E → Q AA sequence (Ref. 2) Curated1
Sequence conflicti19Missing AA sequence (Ref. 2) Curated1
Sequence conflicti25T → L AA sequence (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ237696 Genomic DNA. Translation: CAB40191.1.
RefSeqiWP_000090315.1. NZ_MCFM01000008.1.

Genome annotation databases

GeneIDi28379171.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ237696 Genomic DNA. Translation: CAB40191.1.
RefSeqiWP_000090315.1. NZ_MCFM01000008.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XEXX-ray1.90A/B1-693[»]
3ZZ0X-ray2.80A/B1-693[»]
3ZZTX-ray2.95A/B1-693[»]
3ZZUX-ray2.98A/B1-693[»]
ProteinModelPortaliP68790.
SMRiP68790.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93062.SACOL0593.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi28379171.

Phylogenomic databases

eggNOGiENOG4105CEJ. Bacteria.
COG0480. LUCA.

Miscellaneous databases

EvolutionaryTraceiP68790.

Family and domain databases

CDDicd01434. EFG_mtEFG1_IV. 1 hit.
Gene3Di3.30.230.10. 1 hit.
3.30.70.240. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00054_B. EF_G_EF_2_B. 1 hit.
InterProiIPR009022. EFG_III-V.
IPR000640. EFG_V.
IPR004161. EFTu-like_2.
IPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR004540. Transl_elong_EFG/EF2.
IPR005517. Transl_elong_EFG/EF2_IV.
[Graphical view]
PfamiPF00679. EFG_C. 1 hit.
PF14492. EFG_II. 1 hit.
PF03764. EFG_IV. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SMARTiSM00838. EFG_C. 1 hit.
SM00889. EFG_IV. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF54980. SSF54980. 2 hits.
TIGRFAMsiTIGR00484. EF-G. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEFG_STAAU
AccessioniPrimary (citable) accession number: P68790
Secondary accession number(s): P81683, Q9X7M3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.