ID A0A143HGW1_9BACL Unreviewed; 693 AA.
AC A0A143HGW1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-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 ECO:0000313|EMBL:AMX00502.1};
GN ORFNames=ATY39_14415 {ECO:0000313|EMBL:AMX00502.1};
OS Rummeliibacillus stabekisii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Rummeliibacillus.
OX NCBI_TaxID=241244 {ECO:0000313|EMBL:AMX00502.1, ECO:0000313|Proteomes:UP000076021};
RN [1] {ECO:0000313|EMBL:AMX00502.1, ECO:0000313|Proteomes:UP000076021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PP9 {ECO:0000313|EMBL:AMX00502.1,
RC ECO:0000313|Proteomes:UP000076021};
RX PubMed=27231360;
RA da Mota F.F., Vollu R.E., Jurelevicius D., Seldin L.;
RT "Whole-Genome Sequence of Rummeliibacillus stabekisii Strain PP9 Isolated
RT from Antarctic Soil.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|Proteomes:UP000076021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PP9 {ECO:0000313|Proteomes:UP000076021};
RA Ploux O.;
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}.
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DR EMBL; CP014806; AMX00502.1; -; Genomic_DNA.
DR RefSeq; WP_066790937.1; NZ_CP014806.1.
DR AlphaFoldDB; A0A143HGW1; -.
DR STRING; 241244.ATY39_14415; -.
DR KEGG; rst:ATY39_14415; -.
DR OrthoDB; 2443343at2; -.
DR Proteomes; UP000076021; 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:UP000076021}.
FT DOMAIN 8..283
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 135..138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
SQ SEQUENCE 693 AA; 76698 MW; 021565F0C1480F65 CRC64;
MTREFSLENT RNIGIMAHID AGKTTTTERI LYYTGKIHKI GETHEGASQM DWMEQEQERG
ITITSAATTA QWKGNRVNII DTPGHVDFTV EVERSLRVLD GAVTVLDAQS GVEPQTETVW
RQATTYGVPR IVFINKMDKI GADFLYSVNT LHERLQANAH PIQLPIGAED EFNAIIDLIE
MNATFYKEGD DGSNAEVREI PEEHKAQAEE YREKLIEAVA ELDEDLMEKY FAGEEITNAE
LKAAIRKATL NVEFYPVTCG TAFKNKGVQL MLDAVIDYLP APTDVAAIKG TSVDGDEEIV
RHSSDEEPFS ALAFKVMTDP YVGKLTFFRV YSGILESGSY VQNSSKGKRE RVGRILQMHA
NSREEISKVY AGDIAAAVGL KATTTGDTLC DEKSLVILES MEFPEPVISL SVEPKSKADQ
DKMGQALQKL QEEDPTFRAH TDTETGQTII SGMGELHLDI LVDRMKREFH VEANVGAPQV
SYRETFRSGA QVEGKFVRQS GGRGQFGHVW IEFQPNEEGK GFEFENAIVG GVVPREYIPA
VEAGLRDSLD NGVLAGFPLI DIKAKLFDGS YHDVDSNEMA FKIAASMALK NAVSKCNPVL
LEPVMKVEVV MPEEYLGDIM GNITSRRGRV EGMEARGNAQ VVRAMVPLAE MFGYATTLRS
ATQGRGTFSM VFDHYEEVPK SISEEIIKQN KGA
//
