ID A0A1A9F4Z5_9GAMM Unreviewed; 692 AA.
AC A0A1A9F4Z5;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=A8C75_21685 {ECO:0000313|EMBL:ANG64829.1};
OS Marinobacterium aestuarii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinobacterium.
OX NCBI_TaxID=1821621 {ECO:0000313|EMBL:ANG64829.1, ECO:0000313|Proteomes:UP000078070};
RN [1] {ECO:0000313|Proteomes:UP000078070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST58-10 {ECO:0000313|Proteomes:UP000078070};
RA Baek K., Yang S.-J.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ANG64829.1, ECO:0000313|Proteomes:UP000078070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST58-10 {ECO:0000313|EMBL:ANG64829.1,
RC ECO:0000313|Proteomes:UP000078070};
RX PubMed=29303694; DOI=10.1099/ijsem.0.002561;
RA Bae S.S., Jung J., Chung D., Baek K.;
RT "Marinobacterium aestuarii sp. nov., a benzene-degrading marine bacterium
RT isolated from estuary sediment.";
RL Int. J. Syst. Evol. Microbiol. 68:651-656(2018).
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; CP015839; ANG64829.1; -; Genomic_DNA.
DR RefSeq; WP_067386482.1; NZ_CP015839.1.
DR AlphaFoldDB; A0A1A9F4Z5; -.
DR STRING; 1821621.A8C75_21685; -.
DR KEGG; mars:A8C75_21685; -.
DR OrthoDB; 9804431at2; -.
DR Proteomes; UP000078070; 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: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:UP000078070}.
FT DOMAIN 9..283
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 18..25
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 82..86
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 136..139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
SQ SEQUENCE 692 AA; 76180 MW; A925BBB6DA30D4B7 CRC64;
MDKRHFEPEK IRNIGIIAHI DAGKTTATER MLFYSGITHK LGSVDDGTTT TDWMDQERER
GITIVSAAIT TQWRDHQINI IDTPGHIDFT AEVQRALRVL DGGVVVFDGV HGVESQSETV
WRQAERYRVP RICFINKMDR IGADFQQALA SIRERLHVTP VAVNIPIGAE STFVGVLDLL
DMQQIRWPDE YGAAPVREPI SEALLPAALE ARRELLEAIC ETDDGLLEQY LADEQVAPSQ
WRAGLRRATL ENRLYPVFCG SALRNIGVQP LLDAVVDLLP SPLDRLEVVG HHPVSGEEEH
WKLSLDEPLC ALVFKTVTDP YAGQMAYVRV YSGRLKTGEA VFNPRTGHKL RIGRLVRVFA
DRREDIDTIP AGEIDAVVGL KDAITGDTLC ALDHPLVLES IQFPDPVINI AIEPCAVRDR
DEMNRALAQL KEEDPTFHVH FDDNSGQTIL SGMGELHLEI LMTRIEREHH IKVRSGPPRV
TYKETVAGAV SHIEGRYVHQ SGGHGQFGHV YIDLAPGEPG SGLVFSQQIK GGVIPAAFIT
AVKKGVEEAA QTGLIGGQEV TDVAVTLVDG STHSVDSSEL AFKNAAVQAF RDAALQAQPK
LLEPLCRITV VTPQENLGDV LGQLSARRCE VHSTVPRADG THDVEGLVPL AEMFGYATDL
RSVTQGRALF TLEFDHYAAV PDKVLQKLKL KA
//
