ID   EFTU_HERAU              Reviewed;         400 AA.
AC   P42477;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000255|HAMAP-Rule:MF_00118};
OS   Herpetosiphon aurantiacus (Herpetosiphon giganteus).
OC   Bacteria; Chloroflexi; Chloroflexia; Herpetosiphonales; Herpetosiphonaceae;
OC   Herpetosiphon.
OX   NCBI_TaxID=65;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=HPGA1;
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; X76868; CAA54196.1; -; Genomic_DNA.
DR   AlphaFoldDB; P42477; -.
DR   SMR; P42477; -.
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   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..400
FT                   /note="Elongation factor Tu"
FT                   /id="PRO_0000091335"
FT   DOMAIN          10..209
FT                   /note="tr-type G"
FT   REGION          19..26
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          60..64
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          81..84
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          136..139
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          174..176
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         81..85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         136..139
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   400 AA;  43738 MW;  02A543425AD66686 CRC64;
     MAKQKFERNK PHINIGTIGH VDHGKTTLTA AITKTMALRG RAEFRAFDQI DNAPEERARG
     ITISISHVEY ETENRHYAHV DCPGHADYIK NMITGAAQMD GAILVVSAPD GPMPQTREHI
     LLAGQVEVPA MVVFLNKVDM MDDPELLELV EMELRELLTK YGFPGDEIPI VRGSAKGALD
     SASTDASQPE YQSIQELMQA VDDYIPTPER AIDKPFLMPI EDVFSIKGRG TVVTGRIERG
     IVKVGDTIEI IGMGPDVRTT AVTGVEMFKK LLDEGRAGDN VGALLRGIER TDVERGQVLA
     KPGSIKPHTK FKAEVYVLKK EEGGRHSPFF SGYRPQFYVR TTDVTGAIGL PEGVEMVMPG
     DNIQMTVELI VPVAIEQGLK FAIREGGRTV GAGIVPEIIA