GenomeNet

Database: UniProt
Entry: A0A430K1C2_9FLAO
LinkDB: A0A430K1C2_9FLAO
Original site: A0A430K1C2_9FLAO 
ID   A0A430K1C2_9FLAO        Unreviewed;       710 AA.
AC   A0A430K1C2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 21.
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:RTE52848.1};
GN   ORFNames=EHW67_14365 {ECO:0000313|EMBL:RTE52848.1};
OS   Arenibacter aquaticus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Arenibacter.
OX   NCBI_TaxID=2489054 {ECO:0000313|EMBL:RTE52848.1, ECO:0000313|Proteomes:UP000267585};
RN   [1] {ECO:0000313|EMBL:RTE52848.1, ECO:0000313|Proteomes:UP000267585}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GUO666 {ECO:0000313|EMBL:RTE52848.1,
RC   ECO:0000313|Proteomes:UP000267585};
RA   Guo J., Sun J.;
RT   "Arenibacter aquaticus sp.nov., a marine bacterium isolated from surface
RT   seawater in the South China Sea.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RTE52848.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; RQPJ01000014; RTE52848.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A430K1C2; -.
DR   OrthoDB; 9801591at2; -.
DR   Proteomes; UP000267585; 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: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}.
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   710 AA;  78098 MW;  404F6DE904FD6ACA CRC64;
     MGRDLKYTRN IGIAAHIDAG KTTTTERILF YTGVSHKIGE VHDGAATMDW MEQEQERGIT
     ITSAATTCTW QFPKENGQPT KDAKDYHFNI IDTPGHVDFT VEVNRSLRVL DGLVFLFSAV
     DGVEPQSETN WRLADNYKVP RIGFVNKMDR QGSNFLKVCN QVKTMLGSNA VPIVLPIGDE
     ADFRGIVDLA KNRAIVWHDE NFGATFDVVD IPEEMKAEVK EYRAALIEAV AEYDEALMEK
     FFEDEDSISE EEVHAALRAA VMDRAIIPMV CGSSFKNKGV QFLLDAVCRY LPSPIDKDDI
     VGTDPNTGEA VTRKPDPKEP FAALAFKIAT DPFVGRLAFF RAYSGRLDAG SYILNNRSGK
     KERISRIYQM HSNKQNAIDY IEAGDIGAAV GFKDIKTGDT MSDEKNPIVL ESMDFPDPVI
     GIAVEPKTKA DVDKLGMALG KLAEEDPTFT VRTDEASGQT IISGMGELHL DIIVDRLKRE
     FKVEVSQGEP QVEYKEALTK TAAHREVYKK QSGGRGKFGD IVFEMGPADD DFEGAGLQFI
     DEIKGGRIPK EFIGPVEKGF QAAMKNGPLA GYEMDRMKVV LKDGSFHPVD SDALSFELAA
     KLGYKAAGKA AGAVVMEPIM KLEVLTPEEN MGDIVGDLNR RRGVVTNMDD RAGSKVIKGE
     VPLAEMFGYV TSLRTLSSGR ATSTMEFSHY AETPSNISEE VIKKAKGLTA
//
DBGET integrated database retrieval system