EF2_SULAC
ID EF2_SULAC Reviewed; 737 AA.
AC P23112; Q4JB34;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
GN Name=fusA; Synonyms=fus; OrderedLocusNames=Saci_0603;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-14.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=1900048; DOI=10.1111/j.1432-1033.1991.tb15709.x;
RA Schroeder J., Klink F.;
RT "Gene for the ADP-ribosylatable elongation factor 2 from the extreme
RT thermoacidophilic archaebacterium Sulfolobus acidocaldarius. Cloning,
RT sequencing, comparative analysis.";
RL Eur. J. Biochem. 195:321-327(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY79995.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X54972; CAA38716.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY79995.1; ALT_INIT; Genomic_DNA.
DR PIR; S14408; S14408.
DR RefSeq; WP_015385460.1; NC_007181.1.
DR AlphaFoldDB; P23112; -.
DR SMR; P23112; -.
DR STRING; 330779.Saci_0603; -.
DR EnsemblBacteria; AAY79995; AAY79995; Saci_0603.
DR GeneID; 3473165; -.
DR KEGG; sai:Saci_0603; -.
DR PATRIC; fig|330779.12.peg.582; -.
DR eggNOG; arCOG01559; Archaea.
DR HOGENOM; CLU_002794_11_1_2; -.
DR Proteomes; UP000001018; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
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:1900048"
FT CHAIN 2..737
FT /note="Elongation factor 2"
FT /id="PRO_0000091047"
FT DOMAIN 18..262
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 604
FT /note="Diphthamide"
FT /evidence="ECO:0000250"
FT CONFLICT 138
FT /note="E -> G (in Ref. 1; CAA38716)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 737 AA; 81978 MW; F3D2E2D7FE4077A7 CRC64;
MPRYKTVEQV LSLMKDVTRV RNIGIIAHVD HGKTTTSDTL LAASGIISQK VAGEALALDY
LSVEQQRGIT VKAANISLYH EIDGKGYVIN LIDTPGHVDF SGRVTRSLRV LDGSIVVIDA
VEGIMTQTET VLRQSLEERV RPILFINKVD RLIKELKLSS QEIQKRLIDL IIEVNNLIET
YGEPEFKDQW KIKPELGNVV FGSAKDKWGF SVPMAGKRGV KFSDVVNAYT SGDKAKIEEL
ASKVPIHEAL LDAVIKFVPN PRDSQKYRIP KIWKGDLDSE IAKAMINADP NGPIVMMIND
MKVDPHAGLV ATGRVFSGTL RAGEEVWLVN AKRQQRILQV SLYMGAIREL AEEIPVGNIA
AALGMDAARS GETGVDIRFK DSVLGSFEKL HYISEPVVTI SVEPRNPKDL TKMIDALRKL
SIEDSNLVVK INEETGEYLL SGMGFLHLEV SLQLLKENYG LDVVTTPPIV VYRESIRNKS
QVFEGKSPNK HNKLYISVEP LNNQTIDLIA NGTIKEDMDN KEMAKILRDQ AEWDYDEAKK
IVAIDENINV FIDATSGVQH LREIMDTLLQ GFRLAMKEGP LAFEPVRGVK VVLHDAVVHE
DPAHRGPAQL YPAVRNAIFA GILTSKPTLL EPLQKLDIRI PMEYLGNVTA VITRKRGKVI
NVVQTGNVAR VYAEIPVGES FELASELRAS SAGRAFWGTE FSRWAPVPDS ILVDLIMKIR
ERKGKPKQLP KVEDFIS
