EFTU_BORHD
ID EFTU_BORHD Reviewed; 394 AA.
AC B2S0H9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=BH0476;
OS Borrelia hermsii (strain HS1 / DAH).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX NCBI_TaxID=314723;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS1 / DAH;
RA Porcella S.F., Raffel S.J., Schrumpf M.E., Montgomery B., Smith T.,
RA Schwan T.G.;
RT "The genome sequence of Borrelia hermsii and Borrelia turicatae:
RT comparative analysis of two agents of endemic N. America relapsing fever.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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; CP000048; AAX16985.1; -; Genomic_DNA.
DR RefSeq; WP_012422241.1; NC_010673.1.
DR AlphaFoldDB; B2S0H9; -.
DR SMR; B2S0H9; -.
DR KEGG; bhr:BH0476; -.
DR HOGENOM; CLU_007265_0_0_12; -.
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..394
FT /note="Elongation factor Tu"
FT /id="PRO_1000095052"
FT DOMAIN 10..205
FT /note="tr-type G"
FT REGION 19..26
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 61..65
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 82..85
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 137..140
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 173..175
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 82..86
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 137..140
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ SEQUENCE 394 AA; 43360 MW; 68E9521C8D20B7ED CRC64;
MAKEVFQRTK PHMNVGTIGH VDHGKTTLTA AISIYCSKVN KDAKALKYED IDNAPEEKAR
GITINARHIE YETAGRHYAH VDCPGHADYI KNMITGAAQM DAAILLVAAD SGAEPQTKEH
LLLAQRMGIK KIIVFLNKLD LADPELVELV EVEVLELVEK YGFPGDTPIV KGSAFGAMSN
PDDPEATKCI KELLETMDSY FDLPERDIDK PFLLAIEDVF SISGRGTVAT GRIERGIIKV
GQEVEIVGIR ETRKTTVTGV EMFQKILEQG EAGDNVGLLL RGVDKKDVER GQVIAAIGTI
TPHKKFKASI YCLTKEEGGR HKPFFSGYRP QFFFRTTDVT GMVSLEGKEM VMPGDNVDIV
VELISLIAMD KNVEFAVREG GRTVASGRIL EILE