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Database: UniProt/SWISS-PROT
Entry: EFTU_CORK4
LinkDB: EFTU_CORK4
Original site: EFTU_CORK4 
ID   EFTU_CORK4              Reviewed;         396 AA.
AC   C4LL63;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   16-JAN-2019, entry version 58.
DE   RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000255|HAMAP-Rule:MF_00118};
GN   OrderedLocusNames=ckrop_1849;
OS   Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP
OS   105744 / CCUG 35717).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=645127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717;
RX   PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004;
RA   Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P.,
RA   Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I.,
RA   Goetker S., Weisshaar B., Goesmann A., Droege M., Puehler A.;
RT   "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385
RT   revealed insights into the physiology of a lipophilic corynebacterium
RT   that lacks mycolic acids.";
RL   J. Biotechnol. 136:22-30(2008).
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; CP001620; ACR18568.1; -; Genomic_DNA.
DR   RefSeq; WP_012732455.1; NC_012704.1.
DR   ProteinModelPortal; C4LL63; -.
DR   SMR; C4LL63; -.
DR   STRING; 645127.ckrop_1849; -.
DR   PRIDE; C4LL63; -.
DR   EnsemblBacteria; ACR18568; ACR18568; ckrop_1849.
DR   KEGG; ckp:ckrop_1849; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   OrthoDB; 621774at2; -.
DR   BioCyc; CKRO645127:CKROP_RS09110-MONOMER; -.
DR   Proteomes; UP000001473; 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    396       Elongation factor Tu.
FT                                /FTId=PRO_1000203005.
FT   DOMAIN       10    205       tr-type G.
FT   NP_BIND      19     26       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   NP_BIND      83     87       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   NP_BIND     138    141       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   REGION       19     26       G1. {ECO:0000250}.
FT   REGION       62     66       G2. {ECO:0000250}.
FT   REGION       83     86       G3. {ECO:0000250}.
FT   REGION      138    141       G4. {ECO:0000250}.
FT   REGION      175    177       G5. {ECO:0000250}.
SQ   SEQUENCE   396 AA;  43855 MW;  FB7DAB365C1A01B1 CRC64;
     MAKAKFDRSK PHVNIGTIGH VDHGKTTTTA AITKVLSEKY PEENQAFAFD AIDKAPEEKE
     RGITINIAHV EYSTPKRHYA HVDAPGHADY IKNMITGAAQ MDGAILVVAA TDGPMPQTRE
     HVLLARQVGV PYILVALNKC DMVDDEDLIE LVEMEVRELL AEQDFDEDAP IVHISALKAL
     EGDEKWEQSI LDLMDACDES IPDPVRETDK PFLMPIEDIF TITGRGTVVT GRVERGKLNI
     NDDVEILGIK EKSQNTTVTG IEMFRKQLDY AEAGDNCGLL LRGTKREDVE RGQIVAKPGA
     YTPHTEFEGS VYVLSKDEGG RHTPFFDNYR PQFYFRTTDV TGVVKLPEGT EMVMPGDNVD
     MSVTLIQPVA MDEGLRFAIR EGGRTVGAGR VTKINK
//
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