EFG_MYCMO
ID EFG_MYCMO Reviewed; 694 AA.
AC Q6KHS5;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Elongation factor G {ECO:0000255|HAMAP-Rule:MF_00054};
DE Short=EF-G {ECO:0000255|HAMAP-Rule:MF_00054};
GN Name=fusA {ECO:0000255|HAMAP-Rule:MF_00054}; OrderedLocusNames=MMOB3670;
OS Mycoplasma mobile (strain ATCC 43663 / 163K / NCTC 11711) (Mesomycoplasma
OS mobile).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX NCBI_TaxID=267748;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43663 / 163K / NCTC 11711;
RX PubMed=15289470; DOI=10.1101/gr.2674004;
RA Jaffe J.D., Stange-Thomann N., Smith C., DeCaprio D., Fisher S., Butler J.,
RA Calvo S., Elkins T., FitzGerald M.G., Hafez N., Kodira C.D., Major J.,
RA Wang S., Wilkinson J., Nicol R., Nusbaum C., Birren B., Berg H.C.,
RA Church G.M.;
RT "The complete genome and proteome of Mycoplasma mobile.";
RL Genome Res. 14:1447-1461(2004).
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; AE017308; AAT27853.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6KHS5; -.
DR SMR; Q6KHS5; -.
DR STRING; 267748.MMOB3670; -.
DR PRIDE; Q6KHS5; -.
DR EnsemblBacteria; AAT27853; AAT27853; MMOB3670.
DR KEGG; mmo:MMOB3670; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_14; -.
DR OMA; AATTCHW; -.
DR Proteomes; UP000009072; 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 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..694
FT /note="Elongation factor G"
FT /id="PRO_0000091159"
FT DOMAIN 11..285
FT /note="tr-type G"
FT BINDING 20..27
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 84..88
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 138..141
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ SEQUENCE 694 AA; 76916 MW; E7D10A2F2557709C CRC64;
MIIMAREFEL KDYRNIGIMA HIDAGKTTTT ERILFHTGKI HKIGETHEGA SQMDWMPQEQ
ERGITITSAA TTAFWKGKRI NIIDTPGHVD FTVEVERSLR VLDGAVAVLD AQSGVEPQTE
TVWRQATNYK VPRIVFVNKM DKAGANFDEA VKSVRTRLGG NAVPIQWNIG AESEFQGFID
LVNMEAWIFD GKAEENGQKI AIPTNLVKIA KEKRQELIDA VANYEEDIMM LALEGQDVDN
ETLKKAIRKA TLTSEFFPAV CGSAFKNKGV KAMIDAVIDY LPSPLDVPAI EAHQGENIIT
VKPSDDGDFS ALAFKVMTDP YVGTLTFFRV YSGILNKGSY VINSTKEKKE RIGRILQMHA
NSRTEIEEVR TGDIAAAVGL KDTTTGDTLI GEKAKMFILE KMIFPEPVIS QALEPATKAA
TEKLSLGLQK LSGEDPTFKT YTNEETGQTI IAGMGELHLD IIVDRLRREF GVEVNVGAPQ
VSYRETITAT AEIEGKHIKQ SGGKGQYGHV WIKFEPNHDK GFEFVDKIVG GKIPKEYIKH
VQKGLEEKME IGILAGYPLI DVKATLFDGS YHDVDSSELA YKIAASKALT DGKSKLGATL
LEPIMNVDVV IPEDYFGDIM GDLSRRRGQI KETKTRSDGA STIKANVPLS EMFGYATDLR
SMTAGRGNYQ MIFNHYEKAP KNISDEIIKK RNFN