Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Elongation factor G

Gene

fusA

Organism
Thermus thermophilus
Status
Reviewed-Annotation score: Annotation score: 3 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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 268GTPBy similarity
Nucleotide bindingi83 – 875GTPBy similarity
Nucleotide bindingi137 – 1404GTPBy similarity

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
Gene namesi
Name:fusA
Synonyms:fus
OrganismiThermus thermophilus
Taxonomic identifieri274 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

DrugBankiDB02703. Fusidic Acid.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 691691Elongation factor GPRO_0000091248Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi262724.TTC1331.

Structurei

Secondary structure

1
691
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 113Combined sources
Beta strandi12 – 198Combined sources
Turni21 – 244Combined sources
Helixi25 – 3612Combined sources
Turni39 – 413Combined sources
Beta strandi68 – 747Combined sources
Beta strandi77 – 826Combined sources
Beta strandi86 – 894Combined sources
Helixi91 – 10010Combined sources
Beta strandi102 – 1087Combined sources
Beta strandi112 – 1143Combined sources
Helixi118 – 12710Combined sources
Beta strandi132 – 1365Combined sources
Helixi146 – 15510Combined sources
Beta strandi161 – 1633Combined sources
Beta strandi165 – 1695Combined sources
Helixi171 – 1733Combined sources
Beta strandi176 – 1794Combined sources
Turni180 – 1834Combined sources
Beta strandi184 – 19310Combined sources
Beta strandi196 – 1994Combined sources
Helixi203 – 2053Combined sources
Helixi206 – 22015Combined sources
Helixi221 – 2233Combined sources
Helixi225 – 2339Combined sources
Helixi239 – 25113Combined sources
Beta strandi256 – 2605Combined sources
Turni263 – 2664Combined sources
Helixi269 – 27911Combined sources
Turni283 – 2853Combined sources
Beta strandi289 – 2924Combined sources
Beta strandi298 – 3014Combined sources
Beta strandi305 – 3073Combined sources
Beta strandi310 – 3178Combined sources
Turni320 – 3223Combined sources
Beta strandi325 – 33612Combined sources
Beta strandi340 – 3434Combined sources
Turni344 – 3474Combined sources
Beta strandi348 – 35811Combined sources
Beta strandi363 – 3708Combined sources
Beta strandi374 – 3796Combined sources
Beta strandi388 – 3903Combined sources
Beta strandi392 – 3943Combined sources
Beta strandi398 – 4003Combined sources
Beta strandi409 – 41810Combined sources
Helixi419 – 42911Combined sources
Helixi431 – 4344Combined sources
Beta strandi439 – 4424Combined sources
Beta strandi444 – 4474Combined sources
Beta strandi449 – 4546Combined sources
Helixi456 – 46712Combined sources
Turni468 – 4703Combined sources
Beta strandi474 – 4763Combined sources
Beta strandi479 – 4813Combined sources
Beta strandi484 – 4863Combined sources
Beta strandi491 – 50111Combined sources
Beta strandi504 – 51613Combined sources
Beta strandi523 – 5275Combined sources
Beta strandi531 – 5344Combined sources
Helixi536 – 5383Combined sources
Helixi539 – 55012Combined sources
Turni554 – 5563Combined sources
Beta strandi562 – 57110Combined sources
Turni574 – 5763Combined sources
Helixi579 – 59618Combined sources
Beta strandi600 – 61213Combined sources
Helixi614 – 6163Combined sources
Helixi617 – 62610Combined sources
Beta strandi630 – 6378Combined sources
Beta strandi640 – 6489Combined sources
Helixi649 – 6513Combined sources
Helixi655 – 6628Combined sources
Turni663 – 6653Combined sources
Beta strandi668 – 67811Combined sources
Helixi681 – 6866Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNMX-ray2.80A1-691[»]
1IP8model-H5-689[»]
1IPMmodel-H5-689[»]
1IPOmodel-F5-689[»]
1IPRmodel-F5-689[»]
1JQMelectron microscopy-B1-691[»]
1JQSelectron microscopy-B220-251[»]
C606-673[»]
1KTVX-ray3.80A/B1-691[»]
1PN6electron microscopy10.80A1-691[»]
2BCWelectron microscopy11.20C200-257[»]
2BM0X-ray2.40A1-691[»]
2BM1X-ray2.60A1-691[»]
2BV3X-ray2.50A1-691[»]
2J7KX-ray2.90A1-691[»]
2OM7electron microscopy7.30L1-691[»]
3IZPelectron microscopy-E1-688[»]
4M1KX-ray2.95A1-691[»]
4MYTX-ray3.50A1-691[»]
4MYUX-ray3.00A1-691[»]
DisProtiDP00021.
ProteinModelPortaliP13551.
SMRiP13551. Positions 4-689.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13551.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 284275tr-type GAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CEJ. Bacteria.
COG0480. LUCA.

Family and domain databases

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.
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.

P13551-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVKVEYDLK RLRNIGIAAH IDAGKTTTTE RILYYTGRIH KIGEVHEGAA
60 70 80 90 100
TMDFMEQERE RGITITAAVT TCFWKDHRIN IIDTPGHVDF TIEVERSMRV
110 120 130 140 150
LDGAIVVFDS SQGVEPQSET VWRQAEKYKV PRIAFANKMD KTGADLWLVI
160 170 180 190 200
RTMQERLGAR PVVMQLPIGR EDTFSGIIDV LRMKAYTYGN DLGTDIREIP
210 220 230 240 250
IPEEYLDQAR EYHEKLVEVA ADFDENIMLK YLEGEEPTEE ELVAAIRKGT
260 270 280 290 300
IDLKITPVFL GSALKNKGVQ LLLDAVVDYL PSPLDIPPIK GTTPEGEVVE
310 320 330 340 350
IHPDPNGPLA ALAFKIMADP YVGRLTFIRV YSGTLTSGSY VYNTTKGRKE
360 370 380 390 400
RVARLLRMHA NHREEVEELK AGDLGAVVGL KETITGDTLV GEDAPRVILE
410 420 430 440 450
SIEVPEPVID VAIEPKTKAD QEKLSQALAR LAEEDPTFRV STHPETGQTI
460 470 480 490 500
ISGMGELHLE IIVDRLKREF KVDANVGKPQ VAYRETITKP VDVEGKFIRQ
510 520 530 540 550
TGGRGQYGHV KIKVEPLPRG SGFEFVNAIV GGVIPKEYIP AVQKGIEEAM
560 570 580 590 600
QSGPLIGFPV VDIKVTLYDG SYHEVDSSEM AFKIAGSMAI KEAVQKGDPV
610 620 630 640 650
ILEPIMRVEV TTPEEYMGDV IGDLNARRGQ ILGMEPRGNA QVIRAFVPLA
660 670 680 690
EMFGYATDLR SKTQGRGSFV MFFDHYQEVP KQVQEKLIKG Q
Length:691
Mass (Da):76,879
Last modified:January 1, 1990 - v1
Checksum:i8F0063EE8123470E
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNMX-ray2.80A1-691[»]
1IP8model-H5-689[»]
1IPMmodel-H5-689[»]
1IPOmodel-F5-689[»]
1IPRmodel-F5-689[»]
1JQMelectron microscopy-B1-691[»]
1JQSelectron microscopy-B220-251[»]
C606-673[»]
1KTVX-ray3.80A/B1-691[»]
1PN6electron microscopy10.80A1-691[»]
2BCWelectron microscopy11.20C200-257[»]
2BM0X-ray2.40A1-691[»]
2BM1X-ray2.60A1-691[»]
2BV3X-ray2.50A1-691[»]
2J7KX-ray2.90A1-691[»]
2OM7electron microscopy7.30L1-691[»]
3IZPelectron microscopy-E1-688[»]
4M1KX-ray2.95A1-691[»]
4MYTX-ray3.50A1-691[»]
4MYUX-ray3.00A1-691[»]
DisProtiDP00021.
ProteinModelPortaliP13551.
SMRiP13551. Positions 4-689.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi262724.TTC1331.

Chemistry

DrugBankiDB02703. Fusidic Acid.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CEJ. Bacteria.
COG0480. LUCA.

Miscellaneous databases

EvolutionaryTraceiP13551.

Family and domain databases

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.
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...

Publicationsi

  1. "The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange."
    Al-Karadaghi S., Aevarsson A., Garber M., Zheltonosova J., Liljas A.
    Structure 4:555-565(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
  2. "Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site."
    Laurberg M., Kristensen O., Martemyanov K., Gudkov A.T., Nagaev I., Hughes D., Liljas A.
    J. Mol. Biol. 303:593-603(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT ALA-573.

Entry informationi

Entry nameiEFG_THETH
AccessioniPrimary (citable) accession number: P13551
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: July 6, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

The sequence shown here has been extracted from PDB entry 1KTV.Curated

Keywords - Technical termi

3D-structure

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.