ID   EFTU_STRS2              Reviewed;         398 AA.
AC   A4VZZ3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 83.
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}; OrderedLocusNames=SSU98_0524;
OS   Streptococcus suis (strain 98HAH33).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=391296;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=98HAH33;
RX   PubMed=17375201; DOI=10.1371/journal.pone.0000315;
RA   Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., Pan X.,
RA   Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., Ju A., Ge J.,
RA   Dong Y., Sun W., Jiang Y., Wang J., Yan J., Yang H., Wang X., Gao G.F.,
RA   Yang R., Wang J., Yu J.;
RT   "A glimpse of streptococcal toxic shock syndrome from comparative genomics
RT   of S. suis 2 Chinese isolates.";
RL   PLoS ONE 2:E315-E315(2007).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABP91682.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000408; ABP91682.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A4VZZ3; -.
DR   SMR; A4VZZ3; -.
DR   PRIDE; A4VZZ3; -.
DR   KEGG; ssv:SSU98_0524; -.
DR   HOGENOM; CLU_007265_0_1_9; -.
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..398
FT                   /note="Elongation factor Tu"
FT                   /id="PRO_0000337556"
FT   DOMAIN          10..207
FT                   /note="tr-type G"
FT   REGION          19..26
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          63..67
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          84..87
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          139..142
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          177..179
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         84..88
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         139..142
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   398 AA;  44047 MW;  ED076CD11E42CAA2 CRC64;
     MAKEKYDRSK PHVNIGTIGH VDHGKTTLTA AITTVLARRL PSSVNQPKDY ASIDAAPEER
     ERGITINTAH VEYETEKRHY AHIDAPGHAD YVKNMITGAA QMDGAILVVA STDGPMPQTR
     EHILLSRQVG VKHLIVFMNK VDLVDDEELL ELVEMEIRDL LSEYDFPGDD LPVIQGSALK
     ALEGDSKYED IVMELMNTVD EYIPEPERDT DKPLLLPVED VFSITGRGTV ASGRIDRGTV
     RVNDEIEIVG LQEEKSKAVV TGVEMFRKQL DEGLAGDNVG VLLRGVQRDE IERGQVISKP
     GSINPHTKFK GEVYILTKEE GGRHTPFFDN YRPQFYFRTT DVTGSIKLPE GTEMVMPGDN
     VTIDVELIHP IAVEQGTTFS IREGGRTVGS GMVTEIEA