ID G2Z4A7_FLABF Unreviewed; 718 AA.
AC G2Z4A7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
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 ECO:0000313|EMBL:CCB70599.1};
GN OrderedLocusNames=FBFL15_2602 {ECO:0000313|EMBL:CCB70599.1};
OS Flavobacterium branchiophilum (strain FL-15).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1034807 {ECO:0000313|EMBL:CCB70599.1, ECO:0000313|Proteomes:UP000009186};
RN [1] {ECO:0000313|EMBL:CCB70599.1, ECO:0000313|Proteomes:UP000009186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FL-15 {ECO:0000313|EMBL:CCB70599.1,
RC ECO:0000313|Proteomes:UP000009186};
RX PubMed=21926215; DOI=10.1128/AEM.05625-11;
RG 1:IP;
RG Microbial Evolutionary Genomics,F-75015 Paris;
RG France 2:CNRS;
RG URA2171;
RG F-75015 Paris,France 3:Unite de Virologie et Immunologie Mol.;
RG INRA,78352 Jouy en Josas Cedex;
RG France. 4:Unite de Mathemathique;
RG Informatique et Genome,INRA;
RG 78352 Jouy en Josas Cedex;
RG France. 5:CEA/Genoscope;
RG Evry;
RG France;
RA Touchon M., Barbier P., Bernardet J.F., Loux V., Vacherie B., Barbe V.,
RA Rocha E.P., Duchaud E.;
RT "Complete genome sequence of the fish pathogen Flavobacterium
RT branchiophilum.";
RL Appl. Environ. Microbiol. 77:7656-7662(2011).
CC -!- FUNCTION: Abolishes the inhibitory effect of tetracyclin on protein
CC synthesis by a non-covalent modification of the ribosomes.
CC {ECO:0000256|ARBA:ARBA00003987}.
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; FQ859183; CCB70599.1; -; Genomic_DNA.
DR RefSeq; WP_014085053.1; NC_016001.1.
DR AlphaFoldDB; G2Z4A7; -.
DR STRING; 1034807.FBFL15_2602; -.
DR KEGG; fbr:FBFL15_2602; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_10; -.
DR Proteomes; UP000009186; 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:UP000009186}.
FT DOMAIN 6..295
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 15..22
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 718 AA; 79423 MW; F571D08DFBEC4F0F CRC64;
MARDLKYTRN IGIAAHIDAG KTTTTERILF YTGKSHKIGE VHDGAATMDW MAQEQERGIT
ITSAATTCEW NFPTEQGKVL PETKPYHFNI IDTPGHVDFT VEVNRSLRVL DGLVFLFSAV
DGVEPQSETN WRLADQYRVP RMGFVNKMDR QGANFLNVCQ QVRDMLKSNA VAITLPIGDE
ADFKGVVDLV KNQAIVWHDA TQGATFDIVD IPADMVDEVK EYRSILIEAV ADYDENLLDK
YMEDENSITE EEINTALRAA TIDMAIIPMI AGSSFKNKGV QFMLDAVCKY LPSPTDKEGI
EGIHPDDAEL LEEDQTKILR RPDVKEPFAA LAFKIATDPF VGRLAFFRAY SGRLDAGSYV
LNTRSGSKER ISRIYQMHAN KQNPIEYIEA GDIGAAVGFK DIKTGDTLCD EKHPIILESM
KFPAPVIGIA IEPKTKADVD KMGMALAKLA EEDPTFTVRT DEASGQTIIS GMGELHLDIL
VDRMKREFKV EVNQGEPQVE YKEAFTKSAQ HREVYKKQSG GRGKFGDIVF RLEPADEVDG
KVPVGLQFVN EVKGGNVPKE YIPSVEKGFR EAMKTGPLAG YQVDSLKVTL LDGSFHPVDS
DALSFELAAR MGYREVAKAA GAVILEPIMK MEVITPEENM GDIVGDINRR RGQVNDMGDR
NGAKTIKADV PLSEMFGYVT TLRTLSSGRA TSTMEFSHYA ETPSNISEAV IKKAKGNA
//
