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Database: UniProt/TrEMBL
Entry: A0A0K1HGI9_9PROT
LinkDB: A0A0K1HGI9_9PROT
Original site: A0A0K1HGI9_9PROT 
ID   A0A0K1HGI9_9PROT        Unreviewed;       399 AA.
AC   A0A0K1HGI9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   22-NOV-2017, entry version 14.
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:AKT91128.1};
GN   ORFNames=CUREO_1286 {ECO:0000313|EMBL:AKT91128.1};
OS   Campylobacter ureolyticus RIGS 9880.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=1032069 {ECO:0000313|EMBL:AKT91128.1};
RN   [1] {ECO:0000313|EMBL:AKT91128.1, ECO:0000313|Proteomes:UP000063971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIGS 9880 {ECO:0000313|EMBL:AKT91128.1,
RC   ECO:0000313|Proteomes:UP000063971};
RX   PubMed=26543122;
RA   Miller W.G., Yee E., On S.L., Andersen L.P., Bono J.L.;
RT   "Complete Genome Sequence of the Campylobacter ureolyticus Clinical
RT   Isolate RIGS 9880.";
RL   Genome Announc. 3:e01291-15(2015).
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; CP012195; AKT91128.1; -; Genomic_DNA.
DR   RefSeq; WP_024962200.1; NZ_CP012195.1.
DR   EnsemblBacteria; AKT91128; AKT91128; CUREO_1286.
DR   KEGG; cure:CUREO_1286; -.
DR   PATRIC; fig|1032069.3.peg.1309; -.
DR   KO; K02358; -.
DR   Proteomes; UP000063971; 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:UP000063971};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:AKT91128.1};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00118};
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;  43534 MW;  B38858E62B08E33A CRC64;
     MAKEKFTRNK PHVNIGTIGH VDHGKTTLTA AISAVLSRKG LAELKDYDNI DNAPEEKDRG
     ITIATSHIEY ETANRHYAHV DCPGHADYVK NMITGAAQMD GAILVVNAAD GPMPQTREHI
     LLSRQVGVPY IVVFLNKADM VDDAELIELV EMEVRELLNE YGFPGDDTPI IVGSALKALE
     EAKAGTEGEW SAKIMELMDA VDSYIPTPQR DTDKPFLMPI EDVFSISGRG TVVTGRVEKG
     VVKVGDTIEI VGIKPTQTTT VTGVEMFRKE MEQGEAGDNV GILLRGTGKD DVERGMVLCK
     PGSITPHSKF EAEVYILTKE EGGRHTPFFN NYRPQFYVRT TDVTGSITLG EGKEMVMPGD
     NVKITVELIH PVALEQGTRF AIREGGRTVG SGVVAKIIE
//
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