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Database: UniProt/TrEMBL
Entry: H2JHJ2_9CLOT
LinkDB: H2JHJ2_9CLOT
Original site: H2JHJ2_9CLOT 
ID   H2JHJ2_9CLOT            Unreviewed;       400 AA.
AC   H2JHJ2;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-SEP-2017, 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=Clo1100_0344 {ECO:0000313|EMBL:AEY64630.1};
OS   Clostridium sp. BNL1100.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=755731 {ECO:0000313|EMBL:AEY64630.1, ECO:0000313|Proteomes:UP000007324};
RN   [1] {ECO:0000313|EMBL:AEY64630.1, ECO:0000313|Proteomes:UP000007324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BNL1100 {ECO:0000313|EMBL:AEY64630.1};
RX   PubMed=23209234; DOI=10.1128/JB.01908-12;
RA   Li L.L., Taghavi S., Izquierdo J.A., van der Lelie D.;
RT   "Complete Genome Sequence of Clostridium sp. Strain BNL1100, a
RT   Cellulolytic Mesophile Isolated from Corn Stover.";
RL   J. Bacteriol. 194:6982-6983(2012).
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; CP003259; AEY64630.1; -; Genomic_DNA.
DR   RefSeq; WP_014312032.1; NC_016791.1.
DR   STRING; 755731.Clo1100_0344; -.
DR   EnsemblBacteria; AEY64630; AEY64630; Clo1100_0344.
DR   KEGG; clb:Clo1100_0344; -.
DR   PATRIC; fig|755731.4.peg.345; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   KO; K02358; -.
DR   OrthoDB; POG091H00LA; -.
DR   Proteomes; UP000007324; 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.
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:UP000007324};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:AEY64630.1};
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   400 AA;  43849 MW;  0B57F8DA681AB461 CRC64;
     MAKAKFERNK PHVNIGTIGH VDHGKTSLTA AITKVLGFSG RAEYKAYDQI DAAPEERERG
     ITINTAHVEY ETETRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLSHQVGVPY IIVFLNKCDM VDDEELIELV EMEVRELLST YEFPGDDTPI VRGSALVALE
     SNSTDINAPE YAPIVALMAE VDKYIPTPER ATDKPFIMPV EDVFSITGRG TVATGRVEKG
     IVKVGDEVEI VGLMEAPKKT VVTGVEMFRK LLDQAQAGDN IGALLRGVQR NEIERGQVLA
     KPGSIKPHTY FEGQVYVLTS AEGGRHKPFF NGYRPQFYFR TTDVTGVIEI PEGTEMVMPG
     DHITMKIKLI TPIAMDEGLK FAIREGGRTV GAGNVSKIIE
//
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