EFTU2_PSET1
ID EFTU2_PSET1 Reviewed; 394 AA.
AC Q3IJV1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Elongation factor Tu 2 {ECO:0000255|HAMAP-Rule:MF_00118};
DE Short=EF-Tu 2 {ECO:0000255|HAMAP-Rule:MF_00118};
GN Name=tuf2 {ECO:0000255|HAMAP-Rule:MF_00118}; Synonyms=tufB;
GN OrderedLocusNames=PSHAa2911;
OS Pseudoalteromonas translucida (strain TAC 125).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=326442;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAC 125;
RX PubMed=16169927; DOI=10.1101/gr.4126905;
RA Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C.,
RA Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z.,
RA Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT Pseudoalteromonas haloplanktis TAC125.";
RL Genome Res. 15:1325-1335(2005).
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; CR954246; CAI87946.1; -; Genomic_DNA.
DR RefSeq; WP_011329538.1; NC_007481.1.
DR AlphaFoldDB; Q3IJV1; -.
DR SMR; Q3IJV1; -.
DR STRING; 326442.PSHAa2911; -.
DR EnsemblBacteria; CAI87946; CAI87946; PSHAa2911.
DR KEGG; pha:PSHAa2911; -.
DR PATRIC; fig|326442.8.peg.2809; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_0_6; -.
DR OMA; ERPHCNV; -.
DR OrthoDB; 621774at2; -.
DR BioCyc; PHAL326442:PSHA_RS14280-MON; -.
DR Proteomes; UP000006843; Chromosome I.
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; 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..394
FT /note="Elongation factor Tu 2"
FT /id="PRO_0000337469"
FT DOMAIN 10..204
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"
SQ SEQUENCE 394 AA; 43281 MW; 4FA4042297B7B617 CRC64;
MAKAKFERVK PHVNVGTIGH VDHGKTTLTA AITNVLAKVY GGVAKDFASI DNAPEERERG
ITISTSHVEY DTPTRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI
LLSRQVGVPY IIVFMNKCDM VDDEELLELV EMEVRELLSE YDFPGDDLPL IQGSALKALE
GEKEWEDKIV ELANALDSYI PEPERDIDKA FIMPIEDVFS IQGRGTVVTG RVEAGIIRIN
DEIEIVGIRD TTKSICTGVE MFRKLLDEGR AGENIGALLR GTKREDVERG QVLAKPGSIK
PHTTFESEVY VLSKDEGGRH TPFFKGYRPQ FYFRTTDVTG DVQLPEGVEM VMPGDNVKMT
VTLIAPIAMD EGLRFAIREG GRTVGAGVVA NIVA