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Database: UniProt
Entry: A0A1I7E2E9_9RHOB
LinkDB: A0A1I7E2E9_9RHOB
Original site: A0A1I7E2E9_9RHOB 
ID   A0A1I7E2E9_9RHOB        Unreviewed;       705 AA.
AC   A0A1I7E2E9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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   ORFNames=SAMN05216236_1422 {ECO:0000313|EMBL:SFU18122.1};
OS   Sedimentitalea nanhaiensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Sedimentitalea.
OX   NCBI_TaxID=999627 {ECO:0000313|EMBL:SFU18122.1, ECO:0000313|Proteomes:UP000182466};
RN   [1] {ECO:0000313|EMBL:SFU18122.1, ECO:0000313|Proteomes:UP000182466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10959 {ECO:0000313|EMBL:SFU18122.1,
RC   ECO:0000313|Proteomes:UP000182466};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FPAW01000042; SFU18122.1; -; Genomic_DNA.
DR   RefSeq; WP_027262216.1; NZ_FPAW01000042.1.
DR   AlphaFoldDB; A0A1I7E2E9; -.
DR   STRING; 999627.SAMN05216236_1422; -.
DR   eggNOG; COG0480; Bacteria.
DR   OrthoDB; 9802948at2; -.
DR   Proteomes; UP000182466; Unassembled WGS sequence.
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:UP000182466}.
FT   DOMAIN          8..294
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         92..96
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT   BINDING         146..149
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   705 AA;  77911 MW;  F48E1160CC31D49A CRC64;
     MARDYPLDRY RNFGIMAHID AGKTTCSERI LFYTGKSHNL GEVHDGAATM DWMEQEQERG
     ITITSAATTT FWERTEDGVT PDTPKHRMNI IDTPGHVDFT IEVERSLAVL DGAVAVLDAN
     AGVEPQTETV WRQADRYKVP RIVFVNKMDK IGADFFNCVK MIKDRTGAIP CPIQIPIGAE
     TELEGMVDLV TMEEWVWAGE DLGASWEKRP IRDSLKDQAE EWRANMIEVA VEMDDDAMEA
     YLEGEEPDVP TLRRLIRAGT LGIKFIPVLC GSAFKNKGVQ PLLNAVIDYL PSPMDVVDYM
     GFKPGDETET RNIPRRADDD MAFSGLAFKI MNDPFVGSLT FTRIYSGKLN KGDTLLNSTK
     GKKERVGRMM MMHSNNREEI TEAFAGDIIA LAGLKDTTTG DTLCAVNDPV VLETMTFPDP
     VIEIAVEPKT KADQEKMSQG LARLAAEDPS FRVETDIESG QTIMKGMGEL HLDILVDRLK
     REFKVEANIG APQVAYRETI GHEVEHTYTH KKQSGGSGQF AEVKLIISPT EPGEGYSFES
     KIVGGAVPKE YIPGVEKGIK SVMDSGPLAG FPVIDFKVAL IDGKFHDVDS SVLAFEIAAR
     MGMREGMRKA GAKMLEPIMK VEVITPEEYT GGIIGDLTSR RGQVTGQETR GNAIAIDAMV
     PLANMFGYIN TLRSMSSGRA NFSMQFDHYD PVPQNISDEI QAKFA
//
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