EFTU_CHLAU
ID EFTU_CHLAU Reviewed; 382 AA.
AC P42472;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE Flags: Fragment;
GN Name=tuf {ECO:0000255|HAMAP-Rule:MF_00118};
OS Chloroflexus aurantiacus.
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=1108;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 636 / OK-70-fl;
RX PubMed=8085791; DOI=10.1007/bf00873088;
RA Ludwig W., Neumaier J., Klugbauer N., Brockmann E., Roller C.,
RA Klugbauer S., Reetz K., Schachtner I., Ludvigsen A., Bachleitner M.,
RA Fischer U., Schleifer K.H.;
RT "Phylogenetic relationships of Bacteria based on comparative sequence
RT analysis of elongation factor Tu and ATP-synthase beta-subunit genes.";
RL Antonie Van Leeuwenhoek 64:285-305(1993).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00118}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00118}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00118}.
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DR EMBL; X76864; CAA54193.1; -; Genomic_DNA.
DR PIR; I40602; I40602.
DR AlphaFoldDB; P42472; -.
DR SMR; P42472; -.
DR PRIDE; P42472; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR CDD; cd01884; EF_Tu; 1.
DR CDD; cd03697; EFTU_II; 1.
DR Gene3D; 3.40.50.300; -; 1.
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 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; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00485; EF-Tu; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN <1..382
FT /note="Elongation factor Tu"
FT /id="PRO_0000091309"
FT DOMAIN <1..190
FT /note="tr-type G"
FT BINDING <1..7
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 62..66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 117..120
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT NON_TER 1
SQ SEQUENCE 382 AA; 41913 MW; B21DA1DBA99BF39F CRC64;
HVDHGKTTLT AAITKVMSLK GAAQFMAYDQ IDNAPEERAR GITIAIRHVE YQTDKRHYAH
VDCPGHADYI KNMITGAAQM DGAILVVSAP DGPMPQTREH ILLARQVQVP AIVVFLNKVD
MMDDPELLEL VELELRELLS KYGFPGDEIP IVRGTARNAL ESPSKDINAP EYKCILELMN
AVDEYIPTPQ RAVDQPFLMP IEDVFGIKGR GTVVTGRIER GKVKVGDTVE IVGMTNDAPR
RTVVTGVEMF QKTLDEGIAG DNVGCLLRGI ERTDVERGQV LCAPGSIKPH KKFEAQVYVL
KKEEGGRHTP FFSGYRPQFY IRTTDVTGAI GLPAGMEMVM PGDNVVMTIE LIVPVAIEEG
LRFAIREGGR TVGAGVVTKI LD