EFTU_SPIAU
ID EFTU_SPIAU Reviewed; 375 AA.
AC P42478;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Elongation factor Tu;
DE Short=EF-Tu;
DE Flags: Fragment;
GN Name=tuf;
OS Spirochaeta aurantia.
OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Spirochaeta.
OX NCBI_TaxID=147;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25082 / DSM 1902 / J1;
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:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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|PROSITE-ProRule:PRU01059}.
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DR EMBL; X76874; CAA54201.1; -; Genomic_DNA.
DR PIR; T10899; T10899.
DR AlphaFoldDB; P42478; -.
DR SMR; P42478; -.
DR PRIDE; P42478; -.
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 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..>375
FT /note="Elongation factor Tu"
FT /id="PRO_0000091387"
FT DOMAIN 10..205
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 19..26
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 60..64
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 81..84
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 136..139
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 173..175
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 19..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 136..139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT NON_TER 375
SQ SEQUENCE 375 AA; 40890 MW; C87EFAF916C7445F CRC64;
MAKQNFVRSK PHINVGAIGH VDHGKTTLTA ALTMYGAKKH GGKVMNYDDI DNAPEEKERG
ITINTRHVEY ESAARHYAHV DCPGHADYVK NMITGAAQMD GAILLVAADS GPEPQTREHI
LLAKQVGVAN LVIFLNKMDL ADPELVELVE MEVRDLLNLY GFDGEKTPFI RGSAFAAMSK
PDDPAATKCL DELLDTMDKY FVIPERALDK PFLMPIEDVF SISGRGTVVT GAIAQGKVKV
GDTVEIVGIK PTQTTVVTGV EMFNKLLDAG QAGDNIGALL RGIEKNQVER GQVLAAPKSI
TPHTNFKATI YCLSKEEGGR HNPFFSGYRP QFYFRTTDVT GTVTLPEGKQ MVMPGDNTEL
VVELITPMDK GSRFA