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Q5SHN5

- EFG_THET8

UniProt

Q5SHN5 - EFG_THET8

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Protein
Elongation factor G
Gene
fusA, fus, TTHA1695
Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - 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.UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 268GTP By similarity
Nucleotide bindingi83 – 875GTP By similarity
Nucleotide bindingi137 – 1404GTP By similarity

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-HAMAP
  2. GTPase activity Source: InterPro
  3. translation elongation factor activity Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1734-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor G
Short name:
EF-G
Gene namesi
Name:fusA
Synonyms:fus
Ordered Locus Names:TTHA1695
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 691691Elongation factor GUniRule annotation
PRO_0000091249Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi300852.TTHA1695.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 113
Beta strandi12 – 198
Helixi21 – 244
Helixi25 – 3612
Turni37 – 415
Helixi49 – 513
Helixi57 – 604
Beta strandi69 – 746
Beta strandi77 – 826
Helixi88 – 903
Helixi91 – 10010
Beta strandi102 – 1098
Turni110 – 1123
Helixi116 – 12712
Beta strandi132 – 1376
Helixi146 – 15510
Beta strandi161 – 1633
Beta strandi165 – 1695
Helixi171 – 1733
Beta strandi176 – 1794
Turni180 – 1834
Beta strandi184 – 1885
Beta strandi190 – 1945
Beta strandi196 – 1994
Helixi203 – 2053
Helixi206 – 22015
Turni221 – 2233
Helixi225 – 2339
Helixi239 – 25113
Beta strandi256 – 2605
Helixi263 – 2653
Helixi269 – 27911
Turni283 – 2853
Beta strandi289 – 2924
Beta strandi294 – 2963
Beta strandi298 – 3014
Beta strandi310 – 31910
Turni320 – 3223
Beta strandi323 – 33816
Beta strandi340 – 3434
Turni344 – 3463
Beta strandi349 – 3513
Beta strandi354 – 3585
Beta strandi363 – 3708
Beta strandi374 – 3785
Beta strandi388 – 3914
Beta strandi409 – 4179
Helixi418 – 4203
Turni426 – 4338
Beta strandi436 – 4383
Beta strandi439 – 4413
Beta strandi444 – 4463
Beta strandi449 – 4546
Helixi458 – 4636
Beta strandi464 – 4674
Beta strandi470 – 4734
Turni474 – 4763
Beta strandi484 – 4863
Beta strandi491 – 4999
Beta strandi502 – 5043
Beta strandi506 – 51611
Beta strandi523 – 5275
Beta strandi531 – 5344
Turni536 – 5383
Helixi539 – 54911
Turni554 – 5563
Beta strandi562 – 5709
Turni574 – 5763
Helixi579 – 59517
Beta strandi600 – 61213
Turni614 – 6185
Helixi619 – 6268
Beta strandi631 – 6377
Beta strandi640 – 6489
Turni649 – 6513
Beta strandi652 – 6543
Helixi655 – 6628
Turni663 – 6653
Beta strandi668 – 67811
Helixi681 – 6888

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DARX-ray2.40A1-691[»]
1EFGX-ray2.70A1-691[»]
1ELOX-ray2.80A1-691[»]
1ZN0electron microscopy15.50B6-688[»]
2EFGX-ray2.60A1-691[»]
2WRIX-ray3.60Y1-691[»]
2WRKX-ray3.60Y1-691[»]
2XSYelectron microscopy7.80Y1-691[»]
2XUYelectron microscopy7.60Y1-691[»]
4B8FX-ray3.70Y1-691[»]
4B8HX-ray3.70Y1-691[»]
4CR1X-ray2.95Y1-691[»]
4JUWX-ray2.86Y10-689[»]
ProteinModelPortaliQ5SHN5.
SMRiQ5SHN5. Positions 4-689.

Miscellaneous databases

EvolutionaryTraceiQ5SHN5.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0480.
HOGENOMiHOG000231587.
KOiK02355.
OMAiSGVQPQT.
OrthoDBiEOG6X6RBF.
PhylomeDBiQ5SHN5.

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.
InterProiIPR000795. EF_GTP-bd_dom.
IPR009022. EFG_III-V.
IPR000640. EFG_V.
IPR027417. P-loop_NTPase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005225. Small_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR004540. Transl_elong_EFG/EF2.
IPR005517. Transl_elong_EFG/EF2_IV.
IPR004161. Transl_elong_EFTu/EF1A_2.
[Graphical view]
PfamiPF00679. EFG_C. 1 hit.
PF14492. EFG_II. 1 hit.
PF03764. EFG_IV. 1 hit.
PF00009. GTP_EFTU. 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.

Q5SHN5-1 [UniParc]FASTAAdd to Basket

« Hide

MAVKVEYDLK RLRNIGIAAH IDAGKTTTTE RILYYTGRIH KIGEVHEGAA    50
TMDFMEQERE RGITITAAVT TCFWKDHRIN IIDTPGHVDF TIEVERSMRV 100
LDGAIVVFDS SQGVEPQSET VWRQAEKYKV PRIAFANKMD KTGADLWLVI 150
RTMQERLGAR PVVMQLPIGR EDTFSGIIDV LRMKAYTYGN DLGTDIREIP 200
IPEEYLDQAR EYHEKLVEVA ADFDENIMLK YLEGEEPTEE ELVAAIRKGT 250
IDLKITPVFL GSALKNKGVQ LLLDAVVDYL PSPLDIPPIK GTTPEGEVVE 300
IHPDPNGPLA ALAFKIMADP YVGRLTFIRV YSGTLTSGSY VYNTTKGRKE 350
RVARLLRMHA NHREEVEELK AGDLGAVVGL KETITGDTLV GEDAPRVILE 400
SIEVPEPVID VAIEPKTKAD QEKLSQALAR LAEEDPTFRV STHPETGQTI 450
ISGMGELHLE IIVDRLKREF KVDANVGKPQ VAYRETITKP VDVEGKFIRQ 500
TGGRGQYGHV KIKVEPLPRG SGFEFVNAIV GGVIPKEYIP AVQKGIEEAM 550
QSGPLIGFPV VDIKVTLYDG SYHEVDSSEM AFKIAGSMAI KEAVQKGDPV 600
ILEPIMRVEV TTPEEYMGDV IGDLNARRGQ ILGMEPRGNA QVIRAFVPLA 650
EMFGYATDLR SKTQGRGSFV MFFDHYQEVP KQVQEKLIKG Q 691
Length:691
Mass (Da):76,879
Last modified:December 21, 2004 - v1
Checksum:i8F0063EE8123470E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X16278 Genomic DNA. Translation: CAA34354.1.
AP008226 Genomic DNA. Translation: BAD71518.1.
X52165 Genomic DNA. Translation: CAA36420.1.
PIRiS15928. EFTWG.
RefSeqiWP_011228848.1. NC_006461.1.
YP_144961.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71518; BAD71518; BAD71518.
GeneIDi3169680.
KEGGittj:TTHA1695.
PATRICi23958345. VBITheThe93045_1665.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X16278 Genomic DNA. Translation: CAA34354.1 .
AP008226 Genomic DNA. Translation: BAD71518.1 .
X52165 Genomic DNA. Translation: CAA36420.1 .
PIRi S15928. EFTWG.
RefSeqi WP_011228848.1. NC_006461.1.
YP_144961.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DAR X-ray 2.40 A 1-691 [» ]
1EFG X-ray 2.70 A 1-691 [» ]
1ELO X-ray 2.80 A 1-691 [» ]
1ZN0 electron microscopy 15.50 B 6-688 [» ]
2EFG X-ray 2.60 A 1-691 [» ]
2WRI X-ray 3.60 Y 1-691 [» ]
2WRK X-ray 3.60 Y 1-691 [» ]
2XSY electron microscopy 7.80 Y 1-691 [» ]
2XUY electron microscopy 7.60 Y 1-691 [» ]
4B8F X-ray 3.70 Y 1-691 [» ]
4B8H X-ray 3.70 Y 1-691 [» ]
4CR1 X-ray 2.95 Y 1-691 [» ]
4JUW X-ray 2.86 Y 10-689 [» ]
ProteinModelPortali Q5SHN5.
SMRi Q5SHN5. Positions 4-689.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 300852.TTHA1695.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD71518 ; BAD71518 ; BAD71518 .
GeneIDi 3169680.
KEGGi ttj:TTHA1695.
PATRICi 23958345. VBITheThe93045_1665.

Phylogenomic databases

eggNOGi COG0480.
HOGENOMi HOG000231587.
KOi K02355.
OMAi SGVQPQT.
OrthoDBi EOG6X6RBF.
PhylomeDBi Q5SHN5.

Enzyme and pathway databases

BioCyci TTHE300852:GH8R-1734-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q5SHN5.
PROi Q5SHN5.

Family and domain databases

Gene3Di 3.30.230.10. 1 hit.
3.30.70.240. 1 hit.
3.40.50.300. 1 hit.
HAMAPi MF_00054_B. EF_G_EF_2_B.
InterProi IPR000795. EF_GTP-bd_dom.
IPR009022. EFG_III-V.
IPR000640. EFG_V.
IPR027417. P-loop_NTPase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005225. Small_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR004540. Transl_elong_EFG/EF2.
IPR005517. Transl_elong_EFG/EF2_IV.
IPR004161. Transl_elong_EFTu/EF1A_2.
[Graphical view ]
Pfami PF00679. EFG_C. 1 hit.
PF14492. EFG_II. 1 hit.
PF03764. EFG_IV. 1 hit.
PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view ]
PRINTSi PR00315. ELONGATNFCT.
SMARTi SM00838. EFG_C. 1 hit.
SM00889. EFG_IV. 1 hit.
[Graphical view ]
SUPFAMi SSF50447. SSF50447. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF54980. SSF54980. 2 hits.
TIGRFAMsi TIGR00484. EF-G. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEi PS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the Thermus thermophilus HB8 gene coding for elongation factor G."
    Yakhnin A.V., Vorozheykina D.P., Matvienko N.I.
    Nucleic Acids Res. 17:8863-8863(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.
  3. "Nucleotide sequence of the Thermus thermophilus HB8 rps12 and rps7 genes coding for the ribosomal proteins S12 and S7."
    Yakhnin A.V., Vorozheykina D.P., Matvienko N.I.
    Nucleic Acids Res. 18:3659-3659(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
  4. "The crystal structure of elongation factor G complexed with GDP, at 2.7-A resolution."
    Czworkowski J., Wang J., Steitz T.A., Moore P.B.
    EMBO J. 13:3661-3668(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
  5. "Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus."
    Aevarsson A., Brazhnikov E., Garber M., Zheltonosova J., Chirgadze Y., Al-Karadaghi S., Svensson L.A., Liljas A.
    EMBO J. 13:3669-3677(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS).

Entry informationi

Entry nameiEFG_THET8
AccessioniPrimary (citable) accession number: Q5SHN5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2005
Last sequence update: December 21, 2004
Last modified: September 3, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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