ID M1NJE4_9CORY Unreviewed; 396 AA.
AC M1NJE4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Elongation factor Tu {ECO:0000256|ARBA:ARBA00029554, ECO:0000256|HAMAP-Rule:MF_00118};
DE Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118};
GN Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118};
GN ORFNames=A605_02420 {ECO:0000313|EMBL:AGF71498.1};
OS Corynebacterium halotolerans YIM 70093 = DSM 44683.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1121362 {ECO:0000313|EMBL:AGF71498.1, ECO:0000313|Proteomes:UP000011723};
RN [1] {ECO:0000313|EMBL:AGF71498.1, ECO:0000313|Proteomes:UP000011723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 70093 {ECO:0000313|EMBL:AGF71498.1};
RX PubMed=23408721;
RA Ruckert C., Albersmeier A., Al-Dilaimi A., Niehaus K., Szczepanowski R.,
RA Kalinowski J.;
RT "Genome sequence of the halotolerant bacterium Corynebacterium halotolerans
RT type strain YIM 70093(T) (= DSM 44683(T)).";
RL Stand. Genomic Sci. 7:284-293(2012).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00118}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00118}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000256|ARBA:ARBA00007249, ECO:0000256|HAMAP-
CC Rule:MF_00118}.
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DR EMBL; CP003697; AGF71498.1; -; Genomic_DNA.
DR RefSeq; WP_015399921.1; NZ_JIAJ01000002.1.
DR AlphaFoldDB; M1NJE4; -.
DR STRING; 1121362.A605_02420; -.
DR KEGG; chn:A605_02420; -.
DR PATRIC; fig|1121362.3.peg.485; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_1_11; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000011723; 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; cd01884; EF_Tu; 1.
DR CDD; cd03697; EFTU_II; 1.
DR CDD; cd03707; EFTU_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR HAMAP; MF_00118_B; EF_Tu_B; 1.
DR InterPro; IPR041709; EF-Tu_GTP-bd.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR033720; EFTU_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR NCBIfam; TIGR00485; EF-Tu; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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_00118};
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW Rule:MF_00118};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00118}; Hydrolase {ECO:0000313|EMBL:AGF71498.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00118};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00118}; Reference proteome {ECO:0000313|Proteomes:UP000011723}.
FT DOMAIN 10..205
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 19..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT BINDING 83..87
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT BINDING 138..141
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ SEQUENCE 396 AA; 43897 MW; 9B5ECBC5D34F3C71 CRC64;
MAKAKFERTK PHVNIGTIGH VDHGKTTTTA AITKVLADAF PDLNESFAFD AIDKAPEEKE
RGITINISHV EYQTEKRHYA HVDAPGHADY IKNMITGAAQ MDGAILVVAA TDGPMPQTRE
HVLLARQVGV PYILVALNKC DMVDDEEIIE LVEMEVRELL AEQDYDEDAP IVHISALKAL
EGDEKWAQSI LELMQACDDS IPDPQRATDQ PFLMPIEDIF TITGRGTVVT GRVERGSLKV
NEDVEIIGIK EKSTNTTVTG IEMFRKLLDY TEAGDNCGLL LRGIKREDVE RGQVIIKPGA
YTPHTQFEGS VYVLSKDEGG RHTPFFDNYR PQFYFRTTDV TGVVKLPEGT EMVMPGDNVE
MSVELIQPVA MDEGLRFAIR EGSRTVGAGR VTKIIK
//
