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Database: UniProt/TrEMBL
Entry: A0A099UY53_9HELI
LinkDB: A0A099UY53_9HELI
Original site: A0A099UY53_9HELI 
ID   A0A099UY53_9HELI        Unreviewed;       399 AA.
AC   A0A099UY53;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   23-MAY-2018, entry version 23.
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   ECO:0000313|EMBL:KGL27701.1};
GN   ORFNames=LS79_07325 {ECO:0000313|EMBL:KGL27701.1}, XJ32_04245
GN   {ECO:0000313|EMBL:AQQ59432.1};
OS   Helicobacter bilis.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=37372 {ECO:0000313|EMBL:KGL27701.1, ECO:0000313|Proteomes:UP000029857};
RN   [1] {ECO:0000313|EMBL:KGL27701.1, ECO:0000313|Proteomes:UP000029857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49320 {ECO:0000313|EMBL:KGL27701.1,
RC   ECO:0000313|Proteomes:UP000029857};
RA   Sheh A., Shen Z., Fox J.G.;
RT   "Genome sequencing of Helicobacter and Campylobacter species isolated
RT   from rodents.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AQQ59432.1, ECO:0000313|Proteomes:UP000188298}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAQJH {ECO:0000313|EMBL:AQQ59432.1,
RC   ECO:0000313|Proteomes:UP000188298};
RA   Conlan S., Thomas P.J., Mullikin J., Palmore T.N., Frank K.M.,
RA   Segre J.A.;
RT   "Whole genome sequencing of Helicobacter bilis strain AAQJH.";
RL   Submitted (FEB-2017) 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; CP019645; AQQ59432.1; -; Genomic_DNA.
DR   EMBL; JRPJ01000002; KGL27701.1; -; Genomic_DNA.
DR   RefSeq; WP_004086477.1; NZ_JRPJ01000002.1.
DR   ProteinModelPortal; A0A099UY53; -.
DR   EnsemblBacteria; KGL27701; KGL27701; LS79_07325.
DR   GeneID; 36113081; -.
DR   KEGG; hbl:XJ32_04245; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   KO; K02358; -.
DR   Proteomes; UP000029857; Unassembled WGS sequence.
DR   Proteomes; UP000188298; 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:UP000029857,
KW   ECO:0000313|Proteomes:UP000188298};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:KGL27701.1};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Hydrolase {ECO:0000313|EMBL:KGL27701.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029857}.
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;  43644 MW;  A0FF05129C115A3E CRC64;
     MAKEKFNRSK PHVNVGTIGH VDHGKTTLSA AISAVLATKG LAELKDYDNI DNAPEEKERG
     ITIATSHIEY ETENRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSASD GPMPQTREHI
     LLSRQVGVPY IVVFLNKQDM LDDPELLELV EMEVRDLLNE YEFPGDDTPI VGGSALKALE
     EAKAGTVGEW GQKILDLMAA VDSYIPTPKR DVDKTFLMPV EDVFSIAGRG TVVTGRIERG
     VVKVGDEVEI VGIRDTQKTT VTGVEMFRKE MDQGEAGDNV GVLLRGTKKE EVERGMVLCK
     PGSITPHKKF EAEIYVLTKD EGGRHTPFHN NYRPQFYVRT TDVTGAIILP EGTELVMPGD
     NVKITVELLN PIALELGTRF AIREGGRTVG AGAVTKIIE
//
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