ID A0A220VET3_9GAMM Unreviewed; 693 AA.
AC A0A220VET3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=CF386_06615 {ECO:0000313|EMBL:ASK78692.1};
OS Paraphotobacterium marinum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Paraphotobacterium.
OX NCBI_TaxID=1755811 {ECO:0000313|EMBL:ASK78692.1, ECO:0000313|Proteomes:UP000242175};
RN [1] {ECO:0000313|EMBL:ASK78692.1, ECO:0000313|Proteomes:UP000242175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSCS20N07D {ECO:0000313|EMBL:ASK78692.1,
RC ECO:0000313|Proteomes:UP000242175};
RX PubMed=27154455; DOI=10.1099/ijsem.0.001142;
RA Huang Z., Dong C., Shao Z.;
RT "Paraphotobacterium marinum gen. nov., sp. nov., a member of the family
RT Vibrionaceae, isolated from surface seawater.";
RL Int. J. Syst. Evol. Microbiol. 66:3050-3056(2016).
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; CP022355; ASK78692.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A220VET3; -.
DR KEGG; pmai:CF386_06615; -.
DR OrthoDB; 9804431at2; -.
DR Proteomes; UP000242175; Chromosome large.
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}; Reference proteome {ECO:0000313|Proteomes:UP000242175}.
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 693 AA; 76570 MW; 74EB806E475980A2 CRC64;
MTDLSKYRNI GIFAHVDAGK TTTTERILKL TGKIHRTGEV HDGAATTDFM EQEQERGITI
QSAATTCFWK DHRMNIIDTP GHVDFTVEVY RSLKVLDGGV GVFCGSGGVE PQSETNWRYA
NDSEVSRIIF VNKLDRMGAD FLRVVEQIKN VLGANPLVMT LPIGREDDFV GVVDLLERKA
YVWDDSGLPE NFEVKEVPED MVDQVEQYRE ELIETAIEQD DDLLEAYMEG EEPTMEQIKS
CIRKGTINLD FFPTYCGSAF KNKGVQLVLD AVIDYLPSPT EVKPQPLTDE DGNETGEFAI
VDPNEPFKAL AFKIMDDRFG ALTFIRVYSG KLNKGETVLN SVTGKTERIG RMVEMHANDR
NEISSCQAGD ILAVVGMKNV QTGHTLCDQK HPAILEPMVF PEPVITIAVK PKDKGASEKM
GVALGKMIAE DPSFVVESDH ETGETILKGM GELHLDIKVD ILKRTHGVEL EVGAPLVAYR
ETITQPIEDT YTHKKQSGGA GQFAKIDYRI KPGEPGSGFQ FSSSVVGGNV PKEYWPAVEK
GFKDMMAEGT LAGYPVLDFE VELYDGSFHA VDSSAVAFEI ASKAAFRQSM PKAGPQLIEP
IMHVDVFTPE DHVGDVIGDL NRRRGMIKDQ EAGTTGVRIK ADVPLSEMFG YIGHLRTMTS
GRGQFSMEFS HYMPCPANVA ETVIEEAKAR KNA
//
