ID   EFTU_PLARO              Reviewed;         397 AA.
AC   P72231; P95543;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 101.
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=tuf1;
OS   Planobispora rosea.
OC   Bacteria; Actinobacteria; Streptosporangiales; Streptosporangiaceae;
OC   Planobispora.
OX   NCBI_TaxID=35762;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 53773 / GE2270;
RX   PubMed=8899707; DOI=10.1111/j.1365-2958.1996.tb02654.x;
RA   Sosio M., Amati G., Cappellano C., Sarubbi E., Monti F., Donadio S.;
RT   "An elongation factor Tu (EF-Tu) resistant to the EF-Tu inhibitor GE2270 in
RT   the producing organism Planobispora rosea.";
RL   Mol. Microbiol. 22:43-51(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND RESISTANCE TO ANTIBIOTICS.
RC   STRAIN=ATCC 53773 / GE2270;
RX   PubMed=9016775; DOI=10.1006/bbrc.1996.5947;
RA   Moehrle V.G., Tieleman L.N., Kraal B.;
RT   "Elongation factor Tu1 of the antibiotic GE2270A producer Planobispora
RT   rosea has an unexpected resistance profile against EF-Tu targeted
RT   antibiotics.";
RL   Biochem. Biophys. Res. Commun. 230:320-326(1997).
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   -!- MISCELLANEOUS: Totally resistant to GE2270A and kirromycin, but
CC       sensitive to pulvomycin. {ECO:0000305|PubMed:9016775}.
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; X98830; CAA67345.1; -; Genomic_DNA.
DR   EMBL; U67308; AAB39605.1; -; Genomic_DNA.
DR   PIR; JC5385; JC5385.
DR   AlphaFoldDB; P72231; -.
DR   SMR; P72231; -.
DR   PRIDE; P72231; -.
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..397
FT                   /note="Elongation factor Tu"
FT                   /id="PRO_0000091362"
FT   DOMAIN          10..206
FT                   /note="tr-type G"
FT   REGION          19..26
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          62..66
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          83..86
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          138..141
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          176..178
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         83..87
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         138..141
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   CONFLICT        6
FT                   /note="L -> F (in Ref. 2; AAB39605)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        112
FT                   /note="D -> A (in Ref. 2; AAB39605)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   397 AA;  43911 MW;  8C97163018149E58 CRC64;
     MAKAKLERTK PHMNIGTIGH IDHGKTTLTA AITKVLHDRY PELNKATPFD KIDKAPEEKA
     RGITISIAHV EYQTEKRHYA HVDCPGHADY VKNMITGAAQ MDGAILVVAA TDGPMPQTKE
     HVLLARQVGV PYIVVALNKA DMVDDEEILE LVELEVRELL SAQEFPGDDL PVVRVSALKA
     LEGDEKWADS IIELMNAVDE NIPEPPRDTD KPFLMPIEDV FSITGRGTVV TGRIERGVVK
     VNEQVDIIGI KSEKTTTTVT SIEMFNKMLD EGHAGDNAAL LLRGIKREQV ERGQCIIKPG
     TTTPHTEFEA QVYILSKDEG GRHTPFFNNY RPQFYFRTTD VTGVVNLPEG TEMVMPGDNT
     EMTVQLIQPI AMEEGLKFAI REGGRTVGAG RVTKILK