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Database: UniProt/SWISS-PROT
Entry: EFTU_BARHE
LinkDB: EFTU_BARHE
Original site: EFTU_BARHE 
ID   EFTU_BARHE              Reviewed;         391 AA.
AC   Q8KHX9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JAN-2019, 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=tufB;
GN   OrderedLocusNames=BH06020;
GN   and
GN   Name=tuf2 {ECO:0000255|HAMAP-Rule:MF_00118}; Synonyms=tufA;
GN   OrderedLocusNames=BH10530;
OS   Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS   (Rochalimaea henselae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=283166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX   PubMed=12140235; DOI=10.1093/oxfordjournals.molbev.a004184;
RA   Amiri H., Alsmark C.M., Andersson S.G.E.;
RT   "Proliferation and deterioration of Rickettsia palindromic elements.";
RL   Mol. Biol. Evol. 19:1234-1243(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic
RT   derivative of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; AY099292; AAM92278.1; -; Genomic_DNA.
DR   EMBL; AY099295; AAM92281.1; -; Genomic_DNA.
DR   EMBL; BX897699; CAF27407.1; -; Genomic_DNA.
DR   EMBL; BX897699; CAF27844.1; -; Genomic_DNA.
DR   RefSeq; WP_011180527.1; NZ_LRIJ02000001.1.
DR   ProteinModelPortal; Q8KHX9; -.
DR   SMR; Q8KHX9; -.
DR   STRING; 283166.BH10530; -.
DR   PaxDb; Q8KHX9; -.
DR   PRIDE; Q8KHX9; -.
DR   EnsemblBacteria; CAF27407; CAF27407; BH06020.
DR   EnsemblBacteria; CAF27844; CAF27844; BH10530.
DR   GeneID; 29621408; -.
DR   KEGG; bhe:BH06020; -.
DR   KEGG; bhe:BH10530; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   Proteomes; UP000000421; 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.
FT   CHAIN         1    391       Elongation factor Tu.
FT                                /FTId=PRO_0000337322.
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;  42866 MW;  50B3D4D08696439B CRC64;
     MAKSKFERTK PHVNIGTIGH VDHGKTSLTA AITKYFGEFK AYDQIDAAPE ERARGITIST
     AHVEYETEKR HYAHVDCPGH ADYVKNMITG AAQMDGAILV VSAADGPMPQ TREHILLARQ
     VGVPAIVVFL NKVDQVDDAE LLELVELEVR ELLSKYDFPG DDIPIVKGSA LAALEDKDKS
     IGEDAVRLLM SEVDNYIPTP ERPVDQPFLM PIEDVFSISG RGTVVTGRVE RGVIKVGEEV
     EIIGIRPTSK TTVTGVEMFR KLLDQGQAGD NIGALLRGID REGIERGQVL AKPASVTPHT
     RFKAEAYILT KDEGGRHTPF FTNYRPQFYF RTTDVTGIVT LPEGTEMVMP GDNVAMDVSL
     IVPIAMEEKL RFAIREGGRT VGAGIVSKII E
//
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