ID A0A1J4PYW2_9ACTN Unreviewed; 708 AA.
AC A0A1J4PYW2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 40.
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 ORFNames=VT52_019375 {ECO:0000313|EMBL:OIK25882.1};
OS Streptomyces malaysiense.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1428626 {ECO:0000313|EMBL:OIK25882.1, ECO:0000313|Proteomes:UP000034838};
RN [1] {ECO:0000313|Proteomes:UP000034838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC136T {ECO:0000313|Proteomes:UP000034838};
RA Lee L.H., Chan K.-G.;
RT "Genome sequencing of Streptomyces sp. MUSC136T.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OIK25882.1, ECO:0000313|Proteomes:UP000034838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC136T {ECO:0000313|Proteomes:UP000034838};
RA Lee L.-H., Ser H.-L.;
RT "Genome sequence of Streptomyces malaysiense MUSC 136.";
RL Submitted (OCT-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|ARBA:ARBA00024731,
CC ECO:0000256|HAMAP-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:OIK25882.1}.
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DR EMBL; LBDA02000047; OIK25882.1; -; Genomic_DNA.
DR RefSeq; WP_046417973.1; NZ_LBDA02000047.1.
DR AlphaFoldDB; A0A1J4PYW2; -.
DR OrthoDB; 9801472at2; -.
DR Proteomes; UP000034838; 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}; Reference proteome {ECO:0000313|Proteomes:UP000034838}.
FT DOMAIN 9..295
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 86..90
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 140..143
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
SQ SEQUENCE 708 AA; 77695 MW; 43C11431E7F85A84 CRC64;
MATTSLDLAK VRNIGIMAHI DAGKTTTTER ILFYTGVSYK IGEVHDGAAT MDWMEQEQER
GITITSAATT CHWPLEDVDH TINIIDTPGH VDFTVEVERS LRVLDGAVTV FDGVAGVEPQ
SETVWRQADR YGVPRICFVN KLDRTGAEFH RCVDMIVDRL GAQPLVMQLP IGAEADFKGV
VDLVTMKAFV WSAEATKGEM YDVVDIPDTH TEAAEEYRGK LLEAVAENDE EIMELYLEGE
EPSVEQLYAA IRRITIASGK SEGTTVTPVF CGTAFKNKGV QPLLDAVVRY LPSPVDIEAI
EGHDVKDPEV VVKRKPSDDE PLSALAFKIM SDPHLGKLTF VRVYSGRLES GSSVLNSVKG
KKERIGKIYR MHANKREEIE SVGAGDIVAV MGLKQTTTGE TLSDDKNPVI LESMDFPAPV
IQVAIEPKSK GDQEKLGVAI QRLAEEDPSF QVHSDEETGQ TIIGGMGELH LEVLVDRMRR
EFRVEANVGK PQVAYRETIR KAVERVDYTH KKQTGGTGQF AKVQIGIEPL EGGDTSYEFV
NKVTGGRIPK EYIPSVDAGA QEAMQFGILA GYEMTGVRVI LHDGAYHEVD SSELAFKIAG
SQAFKEAARK ASPVLLEPMM AVEVTTPEDY MGEVIGDINS RRGQIQAMEE RAGARVVKGL
VPLSEMFGYV GDLRSKTSGR ASYSMQFDSY AEVPRNVAEE IIAKAKGE
//
