ID S5R3E7_9PROT Unreviewed; 700 AA.
AC S5R3E7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
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:AGS06724.1};
GN ORFNames=SSDC_00145 {ECO:0000313|EMBL:AGS06724.1};
OS Candidatus Profftella armatura.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Profftella.
OX NCBI_TaxID=669502 {ECO:0000313|EMBL:AGS06724.1, ECO:0000313|Proteomes:UP000015216};
RN [1] {ECO:0000313|EMBL:AGS06724.1, ECO:0000313|Proteomes:UP000015216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DC {ECO:0000313|EMBL:AGS06724.1,
RC ECO:0000313|Proteomes:UP000015216};
RX PubMed=23850282; DOI=10.1016/j.cub.2013.06.027;
RA Nakabachi A., Ueoka R., Oshima K., Teta R., Mangoni A., Gurgui M.,
RA Oldham N.J., van Echten-Deckert G., Okamura K., Yamamoto K., Inoue H.,
RA Ohkuma M., Hongoh Y., Miyagishima S.Y., Hattori M., Piel J., Fukatsu T.;
RT "Defensive bacteriome symbiont with a drastically reduced genome.";
RL Curr. Biol. 23:1478-1484(2013).
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; CP003468; AGS06724.1; -; Genomic_DNA.
DR RefSeq; WP_020915299.1; NZ_CP041281.1.
DR AlphaFoldDB; S5R3E7; -.
DR STRING; 669502.SSDC_00145; -.
DR KEGG; ssdc:SSDC_00145; -.
DR PATRIC; fig|669502.6.peg.28; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_4; -.
DR OrthoDB; 9804431at2; -.
DR Proteomes; UP000015216; 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:UP000015216}.
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 700 AA; 78143 MW; 5602091A8F8199D3 CRC64;
MERKTPIDRY RNIGISAHID AGKTTTTERI LFYTGVNHKI GEVHDGAATM DWMEQEQERG
ITITSAATTC FWKGMANNFP KHHINIIDTP GHVDFTIEVE RSMRILDGVC MVYCAVGGVQ
PQSETVWRQA NKYKVPRLAF VNKMDRIGAN FFKVYKQIQE RLKANPVPIQ IPIGSEESFN
GVIDLVKMQA IYWDEKSKGV KFDYKDIPES LKEEAKKWRE NILEVVSETS ESLMDKYLEE
SDLNETEIKI AIRKLTIAGE IIPMMCGTAF KNKGVQAMLD GIIEYLPSPV DIPPITGSNV
DNEIVFRQAK DKEKFSALAF KISTDPFVGQ LCFIRCYSGI LHSGDVILNS LKIKKERVGR
IVQMHANQRE EIKKISAGDI AAIVGLKNTT TGDTLCDEKN IIILEQISFP EPVISQAIEP
KTKADQEKMG MALNRLAAED PSFRVRIDEE SCQTIIAGMG ELHLDIIVDR IKREFGVEAT
VGKPQVAYRE TIRRTCKEVE GKFIKQSGGR GQYGHVVLKI EPQIPGKGFE FIDAIKSGVV
PREFIPAVEK GIRDSLNSGV LAGYPVVDVK VTLFYGSYHD VDSNENAFRI AGSMAFKDGC
RRSDPTILEP IMAVDVETPE DYAGAVMGDL ASRRGMIQGM NEISGGGGKI IKAEVPLSKM
FGYSTSLRSI TQGRATYTME FKHYSEIPKN LIDTIINNKI
//
