EFG2_SHEON
ID EFG2_SHEON Reviewed; 697 AA.
AC Q8EIJ7;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Elongation factor G 2 {ECO:0000255|HAMAP-Rule:MF_00054};
DE Short=EF-G 2 {ECO:0000255|HAMAP-Rule:MF_00054};
GN Name=fusB; Synonyms=fusA-2; OrderedLocusNames=SO_0842;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014299; AAN53918.1; -; Genomic_DNA.
DR RefSeq; NP_716473.1; NC_004347.2.
DR RefSeq; WP_011071132.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EIJ7; -.
DR SMR; Q8EIJ7; -.
DR STRING; 211586.SO_0842; -.
DR PaxDb; Q8EIJ7; -.
DR KEGG; son:SO_0842; -.
DR PATRIC; fig|211586.12.peg.806; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_6; -.
DR OMA; STTDFME; -.
DR OrthoDB; 88967at2; -.
DR PhylomeDB; Q8EIJ7; -.
DR BioCyc; SONE211586:G1GMP-784-MON; -.
DR Proteomes; UP000008186; 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 GO; GO:0032790; P:ribosome disassembly; IBA:GO_Central.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd01434; EFG_mtEFG1_IV; 1.
DR CDD; cd03713; EFG_mtEFG_C; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR009022; EFG_III.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR035649; EFG_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; IPR004540; Transl_elong_EFG/EF2.
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; TIGR00484; EF-G; 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..697
FT /note="Elongation factor G 2"
FT /id="PRO_0000091210"
FT DOMAIN 5..280
FT /note="tr-type G"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 78..82
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 132..135
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ SEQUENCE 697 AA; 76662 MW; 064D70199A4E4707 CRC64;
MTELSKYRNI GIFAHVDAGK TTTTERILKL TGKIHKIGEV HDGESTTDFM VQEAERGITI
QSAAVSCFWK DHRFNVIDTP GHVDFTVEVY RSLKVLDGGI AVFCGSGGVE PQSETNWRYA
NESEVARIIF VNKLDRMGAD FLRVVKQTKD VLAANPLVMV LPIGIEDEFC GVVDLLTRKA
YVWDDSGIPE NFEVKDVPAN MVDLVEEYRE MLIETAVEQD DDLLEAYMEG EEPSIEDLKR
CIRKGTRTMA FFPTFCGSAF KNKGMQLVLD AVVDYLPAPD EVDPQPLTDE EGNETGEYAI
VSADESLKAL AFKIMDDRFG ALTFVRIYAG RLKKGDTILN SATGKTERIG RMCEMYANDR
IEIESAEAGD IIAIVGMKNV QTGHTLCDVK HPCTLEAMVF PEPVISIAVA PKDKGGSEKM
AIAIGKMIAE DPSFRVETDE DSGETILKGM GELHLDIKVD ILKRTYGVEL IVGEPQVAYR
ETITAMVEDQ YTHKKQSGGS GQFGKIEYII RPGEPNSGFV FKSSVVGGSV PKEFWPAVEK
GFASMMNTGT IAGFPVLDVE FELTDGAYHA VDSSAIAFEI AAKAAFRQSI AKAKPQLLEP
IMKVDVFSPD DNVGDVIGDL NRRRGMIKDQ VAGITGVRVK ADVPLSEMFG YIGSLRTMTS
GRGQFSMEFS HYSPCPNSVA DKVVEQVKER KAAEAKK
