ID A0A1N6VK25_9GAMM Unreviewed; 697 AA.
AC A0A1N6VK25; A0A379ZBQ3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
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_1 {ECO:0000313|EMBL:SUI58557.1};
GN Synonyms=fusA {ECO:0000256|HAMAP-Rule:MF_00054};
GN ORFNames=NCTC10736_00050 {ECO:0000313|EMBL:SUI58557.1};
OS Shewanella morhuae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=365591 {ECO:0000313|EMBL:SUI58557.1, ECO:0000313|Proteomes:UP000255061};
RN [1] {ECO:0000313|EMBL:SUI58557.1, ECO:0000313|Proteomes:UP000255061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10736 {ECO:0000313|EMBL:SUI58557.1,
RC ECO:0000313|Proteomes:UP000255061};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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; UGYV01000001; SUI58557.1; -; Genomic_DNA.
DR RefSeq; WP_076497725.1; NZ_UGYV01000001.1.
DR AlphaFoldDB; A0A1N6VK25; -.
DR STRING; 365591.SAMN05421840_104104; -.
DR OrthoDB; 9804431at2; -.
DR Proteomes; UP000255061; 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:SF5; ELONGATION FACTOR G 1; 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}.
FT DOMAIN 5..280
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 78..82
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 132..135
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
SQ SEQUENCE 697 AA; 76587 MW; 21AF605AB10C64CB CRC64;
MTELSKYRNI GIFAHVDAGK TTTTERILKL TGRIHKAGET HDGESTTDFM VQEAERGITI
QSAAVSCFWK DHRFNVIDTP GHVDFTVEVY RSLKVLDGGI GVFCGSGGVE PQSETNWRYA
NDSEVARIIF VNKLDRIGAD FLRVVKQTKD VLAANPLVMV LPIGAEDQFV GVVDLLTRQA
YVWDDSGLPE NFSIQDVPAD MVDMVEEYRE MLIETAVEQD DAIMEAYMEG EEPSIEDIKR
CIRIGTRTMA LFPTYCGSAF KNKGMQLILD AVVDYLPSPE EVDPQPLTDE EGNETGEFAI
VSADLPLKAL AFKIMDDRFG ALTFVRIYSG RLKKGDTILN SATGKTERIG RMCEMHADDR
IEIESAQAGD IIAIVGMKNV QTGHTLCDVK HPCTLEAMVF PEPVISIAVA PKDKGGSEKM
GVAIGKMIAE DPSFRVETDE DSGETILKGM GELHLDIKVD ILRRTYGVEL IVGEPQVAYR
ETITQMVEDQ YTHKKQSGGS GQFGKIEYII RPGEQNTGFV FKSTVVGGSV PKEFWPAVEK
GFASMMNTGT IAGFPVLDVE FELTDGAFHA VDSSAIAFEI AAKGAFRQSI PKAKPQLLEP
IMKVDVFSPD DNVGDVIGDL NRRRGMIKDQ VAGVTGVRVK ADVPLSEMFG YIGTLRTMTS
GRGQFSMEFS HYSQCPASVA EKVVTQVKER KAAEAKK
//
