EF2_SACS2
ID EF2_SACS2 Reviewed; 736 AA.
AC P30925;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
GN Name=fusA; Synonyms=fus; OrderedLocusNames=SSO0728; ORFNames=C10_002;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 5833 / MT-4;
RX PubMed=8294039; DOI=10.1016/0378-1119(93)90445-9;
RA de Vendittis E., Amatruda M.R., Masullo M., Bocchini V.;
RT "Cloning and sequencing of the gene encoding thermostable elongation factor
RT 2 in Sulfolobus solfataricus.";
RL Gene 136:41-48(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=10701121; DOI=10.1139/g99-108;
RA Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C.,
RA Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D., Gaasterland T.,
RA Garrett R.A., Gordon P., Jeffries A.C., Kozera C., Kushwaha N., Lafleur E.,
RA Medina N., Peng X., Penny S.L., She Q., St Jean A., van der Oost J.,
RA Young F., Zivanovic Y., Doolittle W.F., Ragan M.A., Sensen C.W.;
RT "Gene content and organization of a 281-kbp contig from the genome of the
RT extremely thermophilic archaeon, Sulfolobus solfataricus P2.";
RL Genome 43:116-136(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [4]
RP PROTEIN SEQUENCE OF 2-23 AND 590-604, AND DIPHTHAMIDE AT HIS-603.
RC STRAIN=DSM 5833 / MT-4;
RX PubMed=1390884; DOI=10.1016/0167-4781(92)90002-h;
RA Raimo G., Masullo M., Parente A., Dello Russo A., Bocchini V.;
RT "Molecular, functional and structural properties of an archaebacterial
RT elongation factor 2.";
RL Biochim. Biophys. Acta 1132:127-132(1992).
CC -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC during translation elongation. During this step, the ribosome changes
CC from the pre-translocational (PRE) to the post-translocational (POST)
CC state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound
CC deacylated tRNA move to the P and E sites, respectively. Catalyzes the
CC coordinated movement of the two tRNA molecules, the mRNA and
CC conformational changes in the ribosome.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000305}.
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DR EMBL; X69297; CAA49157.1; -; Genomic_DNA.
DR EMBL; Y18930; CAB57575.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK41025.1; -; Genomic_DNA.
DR PIR; S31809; S31809.
DR RefSeq; WP_009991295.1; NC_002754.1.
DR AlphaFoldDB; P30925; -.
DR SMR; P30925; -.
DR STRING; 273057.SSO0728; -.
DR EnsemblBacteria; AAK41025; AAK41025; SSO0728.
DR GeneID; 44129724; -.
DR KEGG; sso:SSO0728; -.
DR PATRIC; fig|273057.12.peg.725; -.
DR eggNOG; arCOG01559; Archaea.
DR HOGENOM; CLU_002794_11_1_2; -.
DR InParanoid; P30925; -.
DR OMA; GVMTQTE; -.
DR PhylomeDB; P30925; -.
DR BRENDA; 3.6.5.3; 6163.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00054_A; EF_G_EF_2_A; 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR004543; Transl_elong_EFG/EF2_arc.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00490; aEF-2; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1390884"
FT CHAIN 2..736
FT /note="Elongation factor 2"
FT /id="PRO_0000091048"
FT DOMAIN 18..234
FT /note="tr-type G"
FT BINDING 27..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 93..97
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 147..150
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 603
FT /note="Diphthamide"
FT /evidence="ECO:0000269|PubMed:1390884"
SQ SEQUENCE 736 AA; 81820 MW; 06A96231E6EE83E6 CRC64;
MPRYKTVEQV LSLMKDRTRV RNIGIIAHVD HGKTTTSDTL LAASGIISPK VAGEALALDY
LNVEQQRGIT VKAANISLYH EAEGKGYVIN LIDTPGHVDF SGRVTRSLRV LDGSIVVVDA
VEGIMTQTET VLRQSLEERV RPILFINKVD RLVKELKLSP QEMLNRLLDI IRQVNNLIDM
YGEPEFKEKW MINPQAGNVI FGSAKDKWGF SLPMAQKKGI NMKNVIDAYT ASDKSKLEEL
AAQAPINEAL LDAAIKFVPN PIEAQKYRIP KIWKGDLDNE LAKAMLNADP NGPIVFMITD
MKVDPHAGLV ATGRVFSGTL RSGEELWLVN AKTSQRILQV SLYMGPTREL AEEIPAGNIA
AVLGLDRARS GETAISVGFS NVQGSFERLH YISEPVVTIA VEPKNPKDLT KMIDALRKLS
IEDPNLVVKI NEETGEYLLS GMGFLHLEVS LQLLRENYGI DVVTTPPIVV YRESIRAKSQ
VFEGKSPNKH NKFYLSVEPL NDKTIELISN GTIREDMDSK EMAKILRDEA SWDYDEAKRI
IAIDENVNVF VDLTSGVQHL REVMDTVLQG FRLAMKEGPL AHEPIRGVKV ILHDAVIHED
PAHRGPAQIY PAVRNSIFAG FLTSRPTLLE PIQKLDIRVP ADLIGNVTAV ITRKRGKILD
VSQIANMSRI TAEIPVSESY DMASELRGST GGRAFWGTEF SRWAPVPDSI LLDVVTKIRE
RKGLPKELPK VEDFLS
