EF2_STAMF
ID EF2_STAMF Reviewed; 736 AA.
AC A3DMV6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Elongation factor 2 {ECO:0000255|HAMAP-Rule:MF_00054};
DE Short=EF-2 {ECO:0000255|HAMAP-Rule:MF_00054};
GN Name=fusA {ECO:0000255|HAMAP-Rule:MF_00054}; OrderedLocusNames=Smar_0866;
OS Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Staphylothermus.
OX NCBI_TaxID=399550;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1;
RX PubMed=19341479; DOI=10.1186/1471-2164-10-145;
RA Anderson I.J., Dharmarajan L., Rodriguez J., Hooper S., Porat I.,
RA Ulrich L.E., Elkins J.G., Mavromatis K., Sun H., Land M., Lapidus A.,
RA Lucas S., Barry K., Huber H., Zhulin I.B., Whitman W.B., Mukhopadhyay B.,
RA Woese C., Bristow J., Kyrpides N.;
RT "The complete genome sequence of Staphylothermus marinus reveals
RT differences in sulfur metabolism among heterotrophic Crenarchaeota.";
RL BMC Genomics 10:145-145(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1;
RX PubMed=21304655; DOI=10.4056/sigs.30527;
RA Anderson I.J., Sun H., Lapidus A., Copeland A., Glavina Del Rio T.,
RA Tice H., Dalin E., Lucas S., Barry K., Land M., Richardson P., Huber H.,
RA Kyrpides N.C.;
RT "Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986
RT type strain F1.";
RL Stand. Genomic Sci. 1:183-188(2009).
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. {ECO:0000255|HAMAP-
CC Rule:MF_00054}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00054}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00054}.
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DR EMBL; CP000575; ABN69966.1; -; Genomic_DNA.
DR RefSeq; WP_011839157.1; NC_009033.1.
DR AlphaFoldDB; A3DMV6; -.
DR SMR; A3DMV6; -.
DR STRING; 399550.Smar_0866; -.
DR EnsemblBacteria; ABN69966; ABN69966; Smar_0866.
DR GeneID; 4907336; -.
DR KEGG; smr:Smar_0866; -.
DR eggNOG; arCOG01559; Archaea.
DR HOGENOM; CLU_002794_11_1_2; -.
DR OMA; GVMTQTE; -.
DR OrthoDB; 1642at2157; -.
DR Proteomes; UP000000254; 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 3: Inferred from homology;
KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..736
FT /note="Elongation factor 2"
FT /id="PRO_1000008886"
FT DOMAIN 18..261
FT /note="tr-type G"
FT BINDING 27..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 93..97
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 147..150
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT MOD_RES 602
FT /note="Diphthamide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ SEQUENCE 736 AA; 82686 MW; 722A26B0BCE058E0 CRC64;
MVRYKQTMEI LKIMRNLEQV RNIGITAHVD HGKTTLSDSL LAAAGIISEK IAGEALALDY
LDVEQRRGIT VKSANISLYH EYKGKPYVIN LIDTPGHVDF SAKTTRAMRV IDGAILVVDA
VEGVMTQTEM YLRAALEERV RPVLFINKVD RLIKELRLSP QEIQQRFVQI IKEVNQLIAM
YADKEFKTKW QLDPAKGQVA FGSARDRWGF TVPMAKQKGI KFSDIVDLYK KGKEALPELQ
KLAPLHEAVL DMVVKFIPNP REAQKYRLPK IWHGDLNSEI GKAMLETDPN GPLVMLVNDV
RIDPHAGLVA TGRVFSGTLR AGEEVWLVNA RMKQKVLQVS LYMGPYRELA DEIVAGNIAA
VLGLDKARAG ETVVAVEYKD MMTPFEKLRM ISEPVVTVAI EPKNPRDLPK LIDALHKLSI
EDPSLVVRIN EETGEYLLSG MGPLHIEIAL TFLKENYGLD VIASQPIIVY RESIRDKSRV
FEGKSPNKHN KLYISVEPLD EKTISLIHDG IITEDMDPKQ RAKVLREEAG WPTDQARRIW
AIDENINVFV DLTTGVQHLR EVKDTIIQGF RLAMREGPLA MEPVRGVKVI LHDAIIHEDP
AHRGPGQIYP AVRNAIYAGM LTAKPTLLEP IQKLDIKAPM EYLGNITTII TKKRGKILQV
LQQGAVARII AEIPVAETFD LAEQLRGATA GKAIWGQEFS RWAPVPDSML LDLVRKIRER
KGLKPEPPRP EDFIGF
