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Database: UniProt/TrEMBL
Entry: H8H6A5_HELPX
LinkDB: H8H6A5_HELPX
Original site: H8H6A5_HELPX 
ID   H8H6A5_HELPX            Unreviewed;       399 AA.
AC   H8H6A5;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   28-MAR-2018, entry version 36.
DE   RecName: Full=Elongation factor Tu {ECO:0000256|HAMAP-Rule:MF_00118, ECO:0000256|RuleBase:RU004061};
DE            Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118};
GN   ORFNames=HPELS_06260 {ECO:0000313|EMBL:AFF20772.1};
OS   Helicobacter pylori ELS37.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1055527 {ECO:0000313|EMBL:AFF20772.1, ECO:0000313|Proteomes:UP000007885};
RN   [1] {ECO:0000313|EMBL:AFF20772.1, ECO:0000313|Proteomes:UP000007885}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ELS37 {ECO:0000313|EMBL:AFF20772.1,
RC   ECO:0000313|Proteomes:UP000007885};
RA   Bertoli M.T., Kersulyte D., Pascasio M.A., Berg D.E.;
RL   Submitted (JUL-2011) 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:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_00118}.
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DR   EMBL; CP002953; AFF20772.1; -; Genomic_DNA.
DR   RefSeq; WP_001040581.1; NC_017063.1.
DR   EnsemblBacteria; AFF20772; AFF20772; HPELS_06260.
DR   KEGG; hpe:HPELS_06260; -.
DR   PATRIC; fig|1055527.3.peg.1253; -.
DR   KO; K02358; -.
DR   Proteomes; UP000007885; 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 {ECO:0000313|Proteomes:UP000007885};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:AFF20772.1};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Hydrolase {ECO:0000313|EMBL:AFF20772.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00118}.
FT   DOMAIN       10    209       Tr-type G. {ECO:0000259|PROSITE:PS51722}.
FT   NP_BIND      19     26       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
FT   NP_BIND      81     85       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
FT   NP_BIND     136    139       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
SQ   SEQUENCE   399 AA;  43638 MW;  B4770619DF7855C7 CRC64;
     MAKEKFNRTK PHVNIGTIGH VDHGKTTLSA AISAVLSLKG LAEMKDYDNI DNAPEEKERG
     ITIATSHIEY ETENRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLSRQVGVPH IVVFLNKQDM VDDQELLELV EMEVRELLSA YEFPGDDTPI VAGSALRALE
     EAKAGNVGEW GEKVLKLMAE VDSYIPTPER DTEKTFLMPV EDVFSIAGRG TVVTGRIERG
     VVKVGDEVEI VGIRATQKTT VTGVEMFRKE LEKGEAGDNV GVLLRGTKKE EVERGMVLCK
     PGSITPHKKF EGEIYVLSKE EGGRHTPFFT NYRPQFYVRT TDVTGSITLP EGVEMVMPGD
     NVKITVELIS PVALELGTKF AIREGGRTVG AGVVSNIIE
//
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