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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)DescriptionActionsGraphical viewLength
Nucleotide bindingi19 – 26GTPBy similarity8
Nucleotide bindingi83 – 87GTPBy similarity5
Nucleotide bindingi137 – 140GTPBy 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
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 databases

DrugBankiDB02703. Fusidic Acid.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000912481 – 691Elongation factor GAdd BLAST691

Proteomic databases

PRIDEiP13551.

Interactioni

Protein-protein interaction databases

STRINGi262724.TTC1331.

Structurei

Secondary structure

1691
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 11Combined sources3
Beta strandi12 – 19Combined sources8
Turni21 – 24Combined sources4
Helixi25 – 36Combined sources12
Turni39 – 41Combined sources3
Beta strandi68 – 74Combined sources7
Beta strandi77 – 82Combined sources6
Beta strandi86 – 89Combined sources4
Helixi91 – 100Combined sources10
Beta strandi102 – 108Combined sources7
Beta strandi112 – 114Combined sources3
Helixi118 – 127Combined sources10
Beta strandi132 – 136Combined sources5
Helixi146 – 155Combined sources10
Beta strandi161 – 163Combined sources3
Beta strandi165 – 169Combined sources5
Helixi171 – 173Combined sources3
Beta strandi176 – 179Combined sources4
Turni180 – 183Combined sources4
Beta strandi184 – 193Combined sources10
Beta strandi196 – 199Combined sources4
Helixi203 – 205Combined sources3
Helixi206 – 220Combined sources15
Helixi221 – 223Combined sources3
Helixi225 – 233Combined sources9
Helixi239 – 251Combined sources13
Beta strandi256 – 260Combined sources5
Turni263 – 266Combined sources4
Helixi269 – 279Combined sources11
Turni283 – 285Combined sources3
Beta strandi289 – 292Combined sources4
Beta strandi298 – 301Combined sources4
Beta strandi305 – 307Combined sources3
Beta strandi310 – 317Combined sources8
Turni320 – 322Combined sources3
Beta strandi325 – 336Combined sources12
Beta strandi340 – 343Combined sources4
Turni344 – 347Combined sources4
Beta strandi348 – 358Combined sources11
Beta strandi363 – 370Combined sources8
Beta strandi374 – 379Combined sources6
Beta strandi388 – 390Combined sources3
Beta strandi392 – 394Combined sources3
Beta strandi398 – 400Combined sources3
Beta strandi409 – 418Combined sources10
Helixi419 – 429Combined sources11
Helixi431 – 434Combined sources4
Beta strandi439 – 442Combined sources4
Beta strandi444 – 447Combined sources4
Beta strandi449 – 454Combined sources6
Helixi456 – 467Combined sources12
Turni468 – 470Combined sources3
Beta strandi474 – 476Combined sources3
Beta strandi479 – 481Combined sources3
Beta strandi484 – 486Combined sources3
Beta strandi491 – 501Combined sources11
Beta strandi504 – 516Combined sources13
Beta strandi523 – 527Combined sources5
Beta strandi531 – 534Combined sources4
Helixi536 – 538Combined sources3
Helixi539 – 550Combined sources12
Turni554 – 556Combined sources3
Beta strandi562 – 571Combined sources10
Turni574 – 576Combined sources3
Helixi579 – 596Combined sources18
Beta strandi600 – 612Combined sources13
Helixi614 – 616Combined sources3
Helixi617 – 626Combined sources10
Beta strandi630 – 637Combined sources8
Beta strandi640 – 648Combined sources9
Helixi649 – 651Combined sources3
Helixi655 – 662Combined sources8
Turni663 – 665Combined sources3
Beta strandi668 – 678Combined sources11
Helixi681 – 686Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13551.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini10 – 284tr-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.

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi262724.TTC1331.

Chemistry databases

DrugBankiDB02703. Fusidic Acid.

Proteomic databases

PRIDEiP13551.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CEJ. Bacteria.
COG0480. LUCA.

Miscellaneous databases

EvolutionaryTraceiP13551.

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_THETH
AccessioniPrimary (citable) accession number: P13551
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: November 2, 2016
This is version 120 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.