ID A0A178K189_9GAMM Unreviewed; 696 AA.
AC A0A178K189;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=A3K86_18885 {ECO:0000313|EMBL:OAN11041.1};
OS Photobacterium jeanii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=858640 {ECO:0000313|EMBL:OAN11041.1, ECO:0000313|Proteomes:UP000078503};
RN [1] {ECO:0000313|EMBL:OAN11041.1, ECO:0000313|Proteomes:UP000078503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R-40508 {ECO:0000313|EMBL:OAN11041.1,
RC ECO:0000313|Proteomes:UP000078503};
RA Li Y.;
RT "Photobacterium proteolyticum sp. nov. a protease producing bacterium
RT isolated from ocean sediments of Laizhou Bay.";
RL Submitted (MAR-2016) 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}.
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:OAN11041.1}.
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DR EMBL; LVHF01000033; OAN11041.1; -; Genomic_DNA.
DR RefSeq; WP_068335040.1; NZ_PYMD01000002.1.
DR AlphaFoldDB; A0A178K189; -.
DR STRING; 858640.A3K86_18885; -.
DR OrthoDB; 9804431at2; -.
DR Proteomes; UP000078503; 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}; Reference proteome {ECO:0000313|Proteomes:UP000078503}.
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 696 AA; 76180 MW; 97FE88012DC8B989 CRC64;
MTDLSKYRNI GIFAHVDAGK TTTTERILKL TGKIHKIGDT HDGSTTTDFM EQEAERGITI
QSAATTCFWN DHRLNIIDTP GHVDFTVEVY RSLKVLDGGV GVFCGSGGVE PQSETNWRYA
NESEVARLIF VNKLDRMGAD FYNVVDQVKN VLGATPLVMT LPIGREDDFV GVVDVLSRQA
FVWDDTGLPE NYEIQDIPAD MVDDVEAYRE ELIETAVEQD DDLMEAYMEG EEPSIEDIKR
CIRKGTRDLA FFPTYCGSAY KNKGVQLVLD AVVDYLPSPT EVDAQPLTNP EDGEPTGEVA
TVSAEEPLRA LAFKIMDDRF GALTFIRIYS GVMKKGDTIL NSATGKTERI GRMVEMHADQ
RNEIDSAQAG DIIAVVGMKN VQTGHTLCDP KHECTLEPMI FPEPVISIAV APKDKGGSEK
MGIAIGKMVA EDPSFQVETD EDSGETILKG MGELHLDIKV DILKRTYGVD LIVGQPQVAY
RETITQAIED SYTHKKQSGG SGQFGKIDYR IKPGEVGSGF KFTSTVVGGN VPKEFWPAVE
KGFEGMMDNG VLAGFPVLDV EVELFDGGFH AVDSSAVAFE IAAKGAFRQS MPKAGAQLLE
PIMHVDVFTP EDHVGDVIGD LNRRRGMIKD QMAGATGVRI KADVPLSEMF GYIGTLRTMT
SGRGQFSMEF SHYAPCPANV AEAVIAEVKE REASKK
//