EFTU2_BARBK
ID EFTU2_BARBK Reviewed; 391 AA.
AC A1USL2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Elongation factor Tu 2 {ECO:0000255|HAMAP-Rule:MF_00118};
DE Short=EF-Tu 2 {ECO:0000255|HAMAP-Rule:MF_00118};
GN Name=tuf2 {ECO:0000255|HAMAP-Rule:MF_00118};
GN OrderedLocusNames=BARBAKC583_0664;
GN and
GN Name=tuf3 {ECO:0000255|HAMAP-Rule:MF_00118};
GN OrderedLocusNames=BARBAKC583_0696;
OS Bartonella bacilliformis (strain ATCC 35685 / NCTC 12138 / KC583).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=360095;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35685 / NCTC 12138 / KC583;
RA Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S.,
RA Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R.,
RA Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J.,
RA Fraser-Ligget C., Seshadri R.;
RL Submitted (DEC-2006) 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; CP000524; ABM44569.1; -; Genomic_DNA.
DR EMBL; CP000524; ABM45676.1; -; Genomic_DNA.
DR RefSeq; WP_005766892.1; NC_008783.1.
DR AlphaFoldDB; A1USL2; -.
DR SMR; A1USL2; -.
DR STRING; 360095.BARBAKC583_0664; -.
DR PRIDE; A1USL2; -.
DR EnsemblBacteria; ABM44569; ABM44569; BARBAKC583_0664.
DR EnsemblBacteria; ABM45676; ABM45676; BARBAKC583_0696.
DR KEGG; bbk:BARBAKC583_0664; -.
DR KEGG; bbk:BARBAKC583_0696; -.
DR PATRIC; fig|360095.6.peg.675; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_1_5; -.
DR OMA; EGDKEWG; -.
DR OrthoDB; 621774at2; -.
DR Proteomes; UP000000643; 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: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; Reference proteome.
FT CHAIN 1..391
FT /note="Elongation factor Tu 2"
FT /id="PRO_0000337321"
FT DOMAIN 10..201
FT /note="tr-type G"
FT REGION 19..26
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 55..59
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 76..79
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 131..134
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 169..171
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 76..80
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 131..134
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ SEQUENCE 391 AA; 42787 MW; 8966A15ED50DE845 CRC64;
MAKSKFERTK PHVNIGTIGH VDHGKTSLTA AITKYFGEFK AYDQIDAAPE ERARGITIST
AHVEYETDQR HYAHVDCPGH ADYVKNMITG AAQMDGAILV VSAADGPMPQ TREHILLARQ
VGVPAIVVFL NKVDQVDDAE LLELVELEVR ELLSKYDFPG DDIPIVKGSA LAALEDSDKS
IGEDAVRLLM SEVDRYIPTP ERPVDQSFLM PIEDVFSISG RGTVVTGRVE RGVVKVGEEI
EIVGIRPTSK TTVTGVEMFR KLLDQGQAGD NIGALLRGID REGIERGQVL AKPGSVTPHT
KFKAEAYILT KDEGGRHTPF FTNYRPQFYF RTTDVTGIVT LPEGTEMVMP GDNVAMDVSL
IVPIAMEEKL RFAIREGGRT VGAGIVSKII E