ID   EFTU_ANAMM              Reviewed;         393 AA.
AC   Q5PBH1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN   Name=tuf1 {ECO:0000255|HAMAP-Rule:MF_00118}; OrderedLocusNames=AM254;
GN   and
GN   Name=tuf2 {ECO:0000255|HAMAP-Rule:MF_00118}; OrderedLocusNames=AM914;
OS   Anaplasma marginale (strain St. Maries).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma.
OX   NCBI_TaxID=234826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=St. Maries;
RX   PubMed=15618402; DOI=10.1073/pnas.0406656102;
RA   Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L.,
RA   Palmer G.H., McGuire T.C., Knowles D.P. Jr.;
RT   "Complete genome sequencing of Anaplasma marginale reveals that the surface
RT   is skewed to two superfamilies of outer membrane proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005).
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; CP000030; AAV86358.1; -; Genomic_DNA.
DR   EMBL; CP000030; AAV86824.1; -; Genomic_DNA.
DR   RefSeq; WP_011114180.1; NC_004842.2.
DR   AlphaFoldDB; Q5PBH1; -.
DR   SMR; Q5PBH1; -.
DR   GeneID; 7398641; -.
DR   KEGG; ama:AM254; -.
DR   KEGG; ama:AM914; -.
DR   HOGENOM; CLU_007265_0_1_5; -.
DR   OMA; EGDKEWG; -.
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..393
FT                   /note="Elongation factor Tu"
FT                   /id="PRO_0000337315"
FT   DOMAIN          6..204
FT                   /note="tr-type G"
FT   REGION          15..22
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          58..62
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          79..82
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          134..137
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          172..174
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         15..22
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         79..83
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         134..137
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   393 AA;  42914 MW;  94CBE49158718175 CRC64;
     MTEGRKPHIN VGTIGHVDHG KTTLTAALTT VLTRRLSGAN KVVKYDEIDK APEERARGIT
     ISTAHVEYET EGRHYAHVDC PGHADYIKNM ITGAAQMDVA ILVVSATDGA MPQTREHILL
     AKQVGVKDIV TWINKCDVVE DEEMLSIVEM EVRELLSNYG YDGDGVDVVR GSAVKALEES
     SDGPWSEKIM ELVGALEKIE LPVREKDKPF LMSVEDVFSI PGRGTVVTGR IERGVIKVGD
     KVDIVGLRDL QSTVCTGVEM FHKALETGEA GDNAGILLRG IKKEDVERGQ VLSAPGQIRS
     YKAFKAEVYI LKKEEGGRHT PFFSNYQPQF YVRTTDVTGS IKLPSGVEMV MPGDNLSIEV
     ALDKPVALDK GLRFAVREGG RTVGSGIITE ILE