ID EFTU_ANAPZ Reviewed; 393 AA.
AC Q2GJ61;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 107.
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}; Synonyms=tuf-1;
GN OrderedLocusNames=APH_0278;
GN and
GN Name=tuf2 {ECO:0000255|HAMAP-Rule:MF_00118}; Synonyms=tuf-2;
GN OrderedLocusNames=APH_1032;
OS Anaplasma phagocytophilum (strain HZ).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma; phagocytophilum group.
OX NCBI_TaxID=212042;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HZ;
RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C.,
RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C.,
RA Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D.,
RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT "Comparative genomics of emerging human ehrlichiosis agents.";
RL PLoS Genet. 2:208-222(2006).
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; CP000235; ABD44063.1; -; Genomic_DNA.
DR EMBL; CP000235; ABD44111.1; -; Genomic_DNA.
DR RefSeq; WP_011450413.1; NC_007797.1.
DR AlphaFoldDB; Q2GJ61; -.
DR SMR; Q2GJ61; -.
DR STRING; 212042.APH_0278; -.
DR PaxDb; 212042-APH_0278; -.
DR EnsemblBacteria; ABD44063; ABD44063; APH_0278.
DR EnsemblBacteria; ABD44111; ABD44111; APH_1032.
DR GeneID; 56368930; -.
DR KEGG; aph:APH_0278; -.
DR KEGG; aph:APH_1032; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_1_5; -.
DR Proteomes; UP000001943; Chromosome.
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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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 CDD; cd03707; EFTU_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
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 NCBIfam; TIGR00485; EF-Tu; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
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; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 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_0000337316"
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; 42858 MW; F07EF9769616EFE6 CRC64;
MTEGRKPHIN VGTIGHVDHG KTTLTAALTT VLARKLSGAN KVVKYDEIDK APEEKARGIT
ISTAHVEYET EGRHYAHVDC PGHADYIKNM ITGAAQMDVA ILVVSATDGA MPQTREHILL
AKQVGVKDIV VWINKCDVVE DEEMLSLVDM EIRELLSQYG YDGDSIDAVR GSAVKALEED
ADGPWSDKIM ELVGALEKIE LPMREKDKPF LMSVEDVFSI PGRGTVVTGR IERGVVRVGD
KIDIVGLREL QSTVCTGVEM FHKALEAGEA GDNAGILLRG IKKEDVERGQ VLSAPGQMKS
YKKFKAEVYV LKKEEGGRHT PFFANYQPQF YVRTTDVTGS ISLPAGVEMV MPGDNLSIEV
ALDKPVAIDK GLRFAVREGG RTVGSGIITE ILE
//
