ID F7WZV7_9GAMM Unreviewed; 703 AA.
AC F7WZV7;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 08-NOV-2023, entry version 68.
DE RecName: Full=Elongation factor G {ECO:0000256|ARBA:ARBA00017872, 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 ECO:0000313|EMBL:AEH39920.1};
GN ORFNames=BCTU_355 {ECO:0000313|EMBL:AEH39920.1};
OS Buchnera aphidicola (Cinara tujafilina).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=261317 {ECO:0000313|EMBL:AEH39920.1, ECO:0000313|Proteomes:UP000006811};
RN [1] {ECO:0000313|EMBL:AEH39920.1, ECO:0000313|Proteomes:UP000006811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cinara tujafilina {ECO:0000313|Proteomes:UP000006811};
RX PubMed=21571878; DOI=10.1128/AEM.00141-11;
RA Lamelas A., Gosalbes M.J., Moya A., Latorre A.;
RT "The genome of Buchnera aphidicola from the aphid Cinara tujafilina
RT provides new clues about the evolutionary history of metabolic losses in
RT bacterial endosymbionts.";
RL Appl. Environ. Microbiol. 77:4446-4454(2011).
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; CP001817; AEH39920.1; -; Genomic_DNA.
DR RefSeq; WP_013878057.1; NC_015662.1.
DR AlphaFoldDB; F7WZV7; -.
DR STRING; 261317.BCTU_355; -.
DR KEGG; baj:BCTU_355; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_6; -.
DR OrthoDB; 9804431at2; -.
DR Proteomes; UP000006811; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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 PRINTS; PR00315; ELONGATNFCT.
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:UP000006811}.
FT DOMAIN 8..290
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 88..92
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 142..145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
SQ SEQUENCE 703 AA; 78810 MW; A526FD1DB29B14D8 CRC64;
MARTTPITQY RNIGISAHID AGKTTTTERI LFYTGVNHKI GEVHDGAATM DWMVQEQERG
ITITSAATTT FWSGMAKQFL SHRINIIDTP GHVDFTIEVE RSMRILDGVV MVYCAVGGVQ
SQSETVWRQA NKYKVPRIAF INKMDRTGAN FLKVVKQIQT RLHTIAVPIQ LAIGSEENFQ
GVVDLIKMKA IQWNDHDQGV TFKYTEIPQD LLLISKKWNK NLIEVAAEAN DELMEKYLDS
EFLSESEIKK GLRLQVLDNK ITLVTCGSAF KNKGVQALLD AIIEYLPSPK DIKMINRSQE
INKIVDNIHY ADDKQPFSAL AFKIASDAFV GNLTFFRVYS GIVRSGDIVF NSVKSHKERF
GRIVQMHANK REEIKEVRAG DIAAAIGLKN VTTGDTLCDI NNPVILEKMD FPDPVISIAV
EPKTKIDQEK MGIALNRLAK EDPSFKVWTD RESHQTIIAG MGELHLEIIV DRMRREFNVE
ANVGQPQVSY RETIRDIAKG VEGKYIKQSG GRGQYGHVVI DLFPSNPKNS GYLFINDIKG
GVIPTEYISA IDKGIQEQLK SGPLAGYPVV DVTVRLYYGS YHDVDSSELA FKLAASYAFK
SAFKLANPTI LEPIMKVEVE TPEDYMGDVI GDINRRRGII EGMNDDLLGG KNIQSYVPLS
EMFGYATDLR SQTQGRASYS MEFFKYSEAP NIICDKIISK RNS
//
