ID   EFTU_NEIGO              Reviewed;         394 AA.
AC   P48864;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 96.
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}; Synonyms=tufA;
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MS11;
RX   PubMed=8828215; DOI=10.1099/00221287-142-9-2481;
RA   Porcella S.F., Belland R.J., Judd R.C.;
RT   "Identification of an EF-Tu protein that is periplasm-associated and
RT   processed in Neisseria gonorrhoeae.";
RL   Microbiology 142:2481-2489(1996).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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; L36380; AAB41517.2; -; Genomic_DNA.
DR   PIR; T10168; T10168.
DR   AlphaFoldDB; P48864; -.
DR   SMR; P48864; -.
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..394
FT                   /note="Elongation factor Tu"
FT                   /id="PRO_0000091355"
FT   DOMAIN          10..204
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   394 AA;  43084 MW;  F96799BE63520444 CRC64;
     MAKEKFERSK PHVNVGTIGH VDHGKTTLTA ALTTILAKKF GGAAKAYDQI DNAPEEKARG
     ITINTSHVEY ETETRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI
     LLARQVGVPY IIVFMNKCDM VDDAELFQLV EMEIRDLLSS YDFPGDDCPI VQGSALKALE
     GDAAYEEKIF ELATALDRYI PTPERAVDKP FLLPIEDVFS ISGRGTVVTG RVERGIIHVG
     DEIEIVGLKE TQKTTCTGVE MFRKLLDEGQ AGDNVGVLLR GTKREDVERG QVLAKRGTIT
     PHTKFKAEVY VLSKEEGGPH TPFFANYRPQ FYFRTTDVTG TITLEKGVEM VMPGENVTIT
     VELIAPIAME EGLRFAIREG GRTVGAGVVS SVIA