ID I6Z6I6_MYCWM Unreviewed; 677 AA.
AC I6Z6I6;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Elongation factor G {ECO:0000256|HAMAP-Rule:MF_00054};
DE Short=EF-G {ECO:0000256|HAMAP-Rule:MF_00054};
GN Name=fusA {ECO:0000256|HAMAP-Rule:MF_00054};
GN OrderedLocusNames=WEN_02095 {ECO:0000313|EMBL:AFN65208.1};
OS Mycoplasma wenyonii (strain Massachusetts) (Eperythrozoon wenyonii).
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=1197325 {ECO:0000313|EMBL:AFN65208.1, ECO:0000313|Proteomes:UP000009005};
RN [1] {ECO:0000313|EMBL:AFN65208.1, ECO:0000313|Proteomes:UP000009005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts {ECO:0000313|EMBL:AFN65208.1,
RC ECO:0000313|Proteomes:UP000009005};
RX PubMed=22965086; DOI=10.1128/JB.01240-12;
RA Dos Santos A.P., Guimaraes A.M., do Nascimento N.C., Sanmiguel P.J.,
RA Messick J.B.;
RT "Complete genome sequence of Mycoplasma wenyonii strain Massachusetts.";
RL J. Bacteriol. 194:5458-5459(2012).
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:0000256|HAMAP-
CC Rule:MF_00054}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|ARBA:ARBA00005870, ECO:0000256|HAMAP-
CC Rule:MF_00054}.
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DR EMBL; CP003703; AFN65208.1; -; Genomic_DNA.
DR AlphaFoldDB; I6Z6I6; -.
DR STRING; 1197325.WEN_02095; -.
DR KEGG; mwe:WEN_02095; -.
DR PATRIC; fig|1197325.3.peg.450; -.
DR HOGENOM; CLU_002794_4_1_14; -.
DR Proteomes; UP000009005; 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; cd01886; EF-G; 1.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd01434; EFG_mtEFG1_IV; 1.
DR CDD; cd03713; EFG_mtEFG_C; 1.
DR CDD; cd04088; EFG_mtEFG_II; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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; IPR047872; EFG_IV.
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_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_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 NCBIfam; TIGR00484; EF-G; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43261:SF1; RIBOSOME-RELEASING FACTOR 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43261; TRANSLATION ELONGATION FACTOR G-RELATED; 1.
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 SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00054};
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW Rule:MF_00054};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00054};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00054};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00054}; Reference proteome {ECO:0000313|Proteomes:UP000009005}.
FT DOMAIN 1..267
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 2..9
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 66..70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 120..123
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
SQ SEQUENCE 677 AA; 75227 MW; 9744E09AE733C0F0 CRC64;
MAHIDAGKTT TSERILYYTG KIHKMGEVHE GSATMDWMEQ EREKGITITS AATTTEWKGV
VLNLIDTPGH VDFTVEVERS LRVLDGAVVV LDGAMGVEPQ TETVWRQANK YAVPRIIFCN
KMDKVGASFQ SSMKSLKDRL NIKFSPIQLN IGNESSFRGI IDLVGFKAYN FKAGVDEEFE
EIPIPEDQLE EVKSLRETLL NEVLVYDDEI LNRFLSGEEV KEEEIKMCIR KATLTGTFFP
VLCGSSFKHK GVKFLLDAIV DYLPSPLDIP TTKAFTRSGD ELTIENKDES DLVAVAFKIA
TDPFVGRLTF IRVYAGKLKK GDTIYNSTRD IKERVGKLVK MHSNHKTEIE EAGTGEICAL
VGPKSLKTGD TITGSPDSDY LLEAMAFTEP VISLAIEPKT KSDQEKLSIV LKKLADEDPT
FKISSDYETG QTLISGMGEL HLEILIDRMR REFGLQVNVG APQVAYRETF TQTKEIEGQY
IKQTGGRGNY GHVWIKYEPN PEKGFEFVDK IVGGKIPKEY IKSIREGLVD AMKAGQLAGY
PVIDIKATLY DGSYHEVDSN EMAFKIAASL SLKEASKRCG SILLEPIMSI EINSPPQYFG
SVMGDVTAKR GLITATELSP SVSTINCKIP LKEMFGYATT LRSLTQGRGV YSMSFSHYQP
LPKHLLKEIP GFISEGK
//
