ID E6TF02_MYCSR Unreviewed; 396 AA.
AC E6TF02;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
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 OrderedLocusNames=Mspyr1_44930 {ECO:0000313|EMBL:ADU01048.1};
OS Mycolicibacterium gilvum (strain DSM 45189 / LMG 24558 / Spyr1)
OS (Mycobacterium gilvum).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=278137 {ECO:0000313|EMBL:ADU01048.1, ECO:0000313|Proteomes:UP000008916};
RN [1] {ECO:0000313|Proteomes:UP000008916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45189 / LMG 24558 / Spyr1
RC {ECO:0000313|Proteomes:UP000008916};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., LaButti K., Ivanova N.M., Mikhailova N.M., Land M., Hauser L.,
RA Koukkou A.I., Drainas C., Kyrpides N., Woyke T.;
RT "Complete sequence of chromosome of Mycobacterium sp. Spyr1.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADU01048.1, ECO:0000313|Proteomes:UP000008916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45189 / LMG 24558 / Spyr1
RC {ECO:0000313|Proteomes:UP000008916};
RX PubMed=22180818;
RA Kallimanis A., Karabika E., Mavromatis K., Lapidus A., Labutti K.M.,
RA Liolios K., Ivanova N., Goodwin L., Woyke T., Velentzas A.D.,
RA Perisynakis A., Ouzounis C.C., Kyrpides N.C., Koukkou A.I., Drainas C.;
RT "Complete genome sequence of Mycobacterium sp. strain (Spyr1) and
RT reclassification to Mycobacterium gilvum Spyr1.";
RL Stand. Genomic Sci. 5:144-153(2011).
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; CP002385; ADU01048.1; -; Genomic_DNA.
DR RefSeq; WP_011895899.1; NC_014814.1.
DR AlphaFoldDB; E6TF02; -.
DR SMR; E6TF02; -.
DR KEGG; msp:Mspyr1_44930; -.
DR HOGENOM; CLU_007265_0_1_11; -.
DR Proteomes; UP000008916; 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};
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}.
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; 43698 MW; 679BD506A0893E48 CRC64;
MAKAKFERTK PHVNIGTIGH VDHGKTTLTA AITKVLHDQY PDLNESRAFD QIDNAPEERQ
RGITINISHV EYQTEKRHYA HVDAPGHADY IKNMITGAAQ MDGAILVVAA TDGPMPQTRE
HVLLARQVGV PYILVALNKA DMVDDEELIE LVEMEVRELL AAQDFDEDAP VVKVSALKAL
EGDEKWVKSV QELMAAVDES IPDPVRETDK PFLMPVEDVF TITGRGTVVT GRVERGVINV
NEEVEIVGIR PTVTKTTVTG VEMFRKLLDQ GQAGDNVGLL VRGIKREDVE RGQVVVKPGT
TTPHTEFEGS VYILSKDEGG RHTPFFNNYR PQFYFRTTDV TGVVTLPEGT EMVMPGDNTD
IAVKLIQPVA MDEGLRFAIR EGGRTVGAGR VTKIIK
//
