EFTU_GLOVI
ID EFTU_GLOVI Reviewed; 409 AA.
AC P50064;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN Name=tufA {ECO:0000255|HAMAP-Rule:MF_00118}; OrderedLocusNames=glr3928;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 90-324.
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=7663757; DOI=10.1006/mpev.1995.1012;
RA Delwiche C.F., Kuhsel M., Palmer J.D.;
RT "Phylogenetic analysis of tufA sequences indicates a cyanobacterial origin
RT of all plastids.";
RL Mol. Phylogenet. Evol. 4:110-128(1995).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC {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}.
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DR EMBL; BA000045; BAC91869.1; -; Genomic_DNA.
DR EMBL; U09433; AAA87693.1; -; Genomic_DNA.
DR RefSeq; NP_926874.1; NC_005125.1.
DR RefSeq; WP_011143916.1; NC_005125.1.
DR AlphaFoldDB; P50064; -.
DR SMR; P50064; -.
DR STRING; 251221.35214501; -.
DR PRIDE; P50064; -.
DR EnsemblBacteria; BAC91869; BAC91869; BAC91869.
DR KEGG; gvi:glr3928; -.
DR PATRIC; fig|251221.4.peg.3961; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_1_3; -.
DR InParanoid; P50064; -.
DR OMA; EGDKEWG; -.
DR OrthoDB; 621774at2; -.
DR PhylomeDB; P50064; -.
DR Proteomes; UP000000557; 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; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR CDD; cd01884; EF_Tu; 1.
DR CDD; cd03697; EFTU_II; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00118_B; EF_Tu_B; 1.
DR InterPro; IPR041709; EF-Tu_GTP-bd.
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; T_Tr_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 Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..409
FT /note="Elongation factor Tu"
FT /id="PRO_0000091330"
FT DOMAIN 10..214
FT /note="tr-type G"
FT REGION 19..26
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 60..64
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 81..84
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 136..139
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 174..176
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 19..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 136..139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT CONFLICT 158
FT /note="Missing (in Ref. 2; AAA87693)"
FT /evidence="ECO:0000305"
FT CONFLICT 228..233
FT /note="VFSITG -> LLVSR (in Ref. 2; AAA87693)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="Missing (in Ref. 2; AAA87693)"
FT /evidence="ECO:0000305"
FT CONFLICT 260..264
FT /note="GTRST -> TRS (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="Missing (in Ref. 2; AAA87693)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 409 AA; 44760 MW; D1290EEA0D4D3CB7 CRC64;
MARAKFERNK PHVNIGTIGH VDHGKTTLTA AITMTLAALG RAKAKKYDEI DQAPEEKARG
ITINTAHVEY ETEKRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
LLARQVGVPN IVVFLNKKDQ LDDPELLELV ELEVRELLSK YDFPGDDVPI VAGSALMALE
KMASEPKLIR GKDDWVDCIY SLMDAVDAYI PTPERAIDKP FLMAVEDVFS ITGRGTVATG
RIERGKVKVG ETIELVGIRG TRSTTVTGLE MFQKSLDEGL AGDNIGVLLR GIKKEDVERG
MVLAKPGSIT PHTQFEGEVY ILSKEEGGRH TPFFAGYRPQ FYVRTTDVTG TIVTFTDDEG
KSAEMVMPGD RIKMTVELIN PIAIEDGMRF AIREGGRTVG AGVVSKILK
