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Q5SHN5

- EFG_THET8

UniProt

Q5SHN5 - EFG_THET8

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Protein

Elongation factor G

Gene

fusA

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.

Regions

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

GO - Molecular functioni

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 691691Elongation factor GPRO_0000091249Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi300852.TTHA1695.

Structurei

Secondary structure

1
691
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 113Combined sources
Beta strandi12 – 198Combined sources
Helixi21 – 244Combined sources
Helixi25 – 3612Combined sources
Turni37 – 415Combined sources
Helixi49 – 513Combined sources
Helixi57 – 604Combined sources
Beta strandi69 – 746Combined sources
Beta strandi77 – 826Combined sources
Helixi88 – 903Combined sources
Helixi91 – 10010Combined sources
Beta strandi102 – 1098Combined sources
Turni110 – 1123Combined sources
Helixi116 – 12712Combined sources
Beta strandi132 – 1376Combined sources
Helixi146 – 15510Combined sources
Beta strandi161 – 1633Combined sources
Beta strandi165 – 1695Combined sources
Helixi171 – 1733Combined sources
Beta strandi176 – 1794Combined sources
Turni180 – 1834Combined sources
Beta strandi184 – 1885Combined sources
Beta strandi190 – 1945Combined sources
Beta strandi196 – 1994Combined sources
Helixi203 – 2053Combined sources
Helixi206 – 22015Combined sources
Turni221 – 2233Combined sources
Helixi225 – 2339Combined sources
Helixi239 – 25113Combined sources
Beta strandi256 – 2605Combined sources
Helixi263 – 2653Combined sources
Helixi269 – 27911Combined sources
Turni283 – 2853Combined sources
Beta strandi289 – 2924Combined sources
Beta strandi294 – 2963Combined sources
Beta strandi298 – 3014Combined sources
Beta strandi310 – 31910Combined sources
Turni320 – 3223Combined sources
Beta strandi323 – 33816Combined sources
Beta strandi340 – 3434Combined sources
Turni344 – 3463Combined sources
Beta strandi349 – 3513Combined sources
Beta strandi354 – 3585Combined sources
Beta strandi363 – 3708Combined sources
Beta strandi374 – 3785Combined sources
Beta strandi388 – 3914Combined sources
Beta strandi409 – 4179Combined sources
Helixi418 – 4203Combined sources
Turni426 – 4338Combined sources
Beta strandi436 – 4383Combined sources
Beta strandi439 – 4413Combined sources
Beta strandi444 – 4463Combined sources
Beta strandi449 – 4546Combined sources
Helixi458 – 4636Combined sources
Beta strandi464 – 4674Combined sources
Beta strandi470 – 4734Combined sources
Turni474 – 4763Combined sources
Beta strandi484 – 4863Combined sources
Beta strandi491 – 4999Combined sources
Beta strandi502 – 5043Combined sources
Beta strandi506 – 51611Combined sources
Beta strandi523 – 5275Combined sources
Beta strandi531 – 5344Combined sources
Turni536 – 5383Combined sources
Helixi539 – 54911Combined sources
Turni554 – 5563Combined sources
Beta strandi562 – 5709Combined sources
Turni574 – 5763Combined sources
Helixi579 – 59517Combined sources
Beta strandi600 – 61213Combined sources
Turni614 – 6185Combined sources
Helixi619 – 6268Combined sources
Beta strandi631 – 6377Combined sources
Beta strandi640 – 6489Combined sources
Turni649 – 6513Combined sources
Beta strandi652 – 6543Combined sources
Helixi655 – 6628Combined sources
Turni663 – 6653Combined sources
Beta strandi668 – 67811Combined sources
Helixi681 – 6888Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ5SHN5.

Family & Domainsi

Domains and Repeats

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

        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:December 21, 2004 - v1
Checksum:i8F0063EE8123470E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 81 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