GenomeNet

Database: UniProt/SWISS-PROT
Entry: EFTU2_BARBK
LinkDB: EFTU2_BARBK
Original site: 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   16-JAN-2019, entry version 82.
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 / KC583).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=360095;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35685 / 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
CC       aminoacyl-tRNA to the A-site of ribosomes during protein
CC       biosynthesis. {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}.
DR   EMBL; CP000524; ABM44569.1; -; Genomic_DNA.
DR   EMBL; CP000524; ABM45676.1; -; Genomic_DNA.
DR   RefSeq; WP_005766892.1; NC_008783.1.
DR   ProteinModelPortal; A1USL2; -.
DR   SMR; A1USL2; -.
DR   STRING; 360095.BARBAKC583_0696; -.
DR   PRIDE; A1USL2; -.
DR   EnsemblBacteria; ABM44569; ABM44569; BARBAKC583_0664.
DR   EnsemblBacteria; ABM45676; ABM45676; BARBAKC583_0696.
DR   GeneID; 4684260; -.
DR   KEGG; bbk:BARBAKC583_0664; -.
DR   KEGG; bbk:BARBAKC583_0696; -.
DR   PATRIC; fig|360095.6.peg.675; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   OrthoDB; 621774at2; -.
DR   BioCyc; BBAC360095:G1G7W-620-MONOMER; -.
DR   BioCyc; BBAC360095:G1G7W-652-MONOMER; -.
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; cd03697; EFTU_II; 1.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1.
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; TF_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   Complete proteome; Cytoplasm; Elongation factor; GTP-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN         1    391       Elongation factor Tu 2.
FT                                /FTId=PRO_0000337321.
FT   DOMAIN       10    201       tr-type G.
FT   NP_BIND      19     26       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   NP_BIND      76     80       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   NP_BIND     131    134       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   REGION       19     26       G1. {ECO:0000250}.
FT   REGION       55     59       G2. {ECO:0000250}.
FT   REGION       76     79       G3. {ECO:0000250}.
FT   REGION      131    134       G4. {ECO:0000250}.
FT   REGION      169    171       G5. {ECO:0000250}.
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
//
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