ID E8WZK7_GRATM Unreviewed; 697 AA.
AC E8WZK7;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
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=AciX9_2958 {ECO:0000313|EMBL:ADW69981.1};
OS Granulicella tundricola (strain ATCC BAA-1859 / DSM 23138 / MP5ACTX9).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Granulicella.
OX NCBI_TaxID=1198114 {ECO:0000313|Proteomes:UP000000343};
RN [1] {ECO:0000313|Proteomes:UP000000343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP5ACTX9 {ECO:0000313|Proteomes:UP000000343};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Ovchinnikova G., Pagani I., Rawat S.R., Mannisto M.,
RA Haggblom M.M., Woyke T.;
RT "Complete sequence of chromosome of Acidobacterium sp. MP5ACTX9.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002480; ADW69981.1; -; Genomic_DNA.
DR RefSeq; WP_013581295.1; NC_015064.1.
DR AlphaFoldDB; E8WZK7; -.
DR STRING; 1198114.AciX9_2958; -.
DR PaxDb; 1198114-AciX9_2958; -.
DR KEGG; acm:AciX9_2958; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_0; -.
DR OrthoDB; 9804431at2; -.
DR Proteomes; UP000000343; 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 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:UP000000343}.
FT DOMAIN 8..283
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 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 135..138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
SQ SEQUENCE 697 AA; 76537 MW; 75286C4BD8A2935F CRC64;
MARTIPLNRC RNIGIMAHID AGKTTTTERI LFYTGITHRI GEVHEGTATM DWMEQEQERG
ITITSAATTC TWKNQRINII DTPGHVDFTA EVERSLRVLD GAVACFDAVA GVQPQSETVW
RQADKYKVPR ICFINKMDKA GADAVYATST IVDRLGARAI PINIQIGAEA KFLGVIDLVT
MKAILWHDET MGAEYSVEEI PAALLETAQK ARAVLIEAVA DSDDEIMNLY LEGEEPTEAQ
LKTGIRKATI AMNIFPVLCG SSFKNKGVQT LLDAVVDYLP SPLDIPPMIG HNPDNMEQEI
IRKADDSEPL SALGFKIMTD PFVGQLIFIR IYSGVLKTGD TTLNPRTGKT ERIGRLLKMH
ANKREEITEI MAGDICAAVG LKNLITGDTI CSEKNPVVLE SIDFPKPVIE VAVEPKTKAD
QEKMGVALAK LAQEDPTFNV RTDVDSGQTI IAGMGELHLE IIVDRMMREY KVEANVGKPQ
VNYRETIRGN ADAEGKYIRQ TGGSGNYGHA KIRLSPNEPG KGYEFSNDTK GGTIPKEYIK
PIDQGIQEAM QGGVLAGYEM VDIKVSLYDG SYHDVDSNEM AFKIAGSMAF KEAARKAKPV
LLEPVMAVEV TVPEDYMGTI IGDLNSRRGR IEGMEMVGNT QAIRASVPLS TMFGYATHMR
GATQGRANYS MQFKQYEEAP RSVSEEIIAK VQGKDSK
//
