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Database: UniProt/TrEMBL
Entry: F2J5R7_POLGS
LinkDB: F2J5R7_POLGS
Original site: F2J5R7_POLGS 
ID   F2J5R7_POLGS            Unreviewed;       396 AA.
AC   F2J5R7;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=Elongation factor Tu {ECO:0000256|ARBA:ARBA00029554, ECO:0000256|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118,
GN   ECO:0000313|EMBL:ADZ70150.1};
GN   OrderedLocusNames=SL003B_1723 {ECO:0000313|EMBL:ADZ70150.1},
GN   SL003B_1737 {ECO:0000313|EMBL:ADZ70163.1};
OS   Polymorphum gilvum (strain LMG 25793 / CGMCC 1.9160 / SL003B-26A1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Polymorphum.
OX   NCBI_TaxID=991905 {ECO:0000313|EMBL:ADZ70150.1, ECO:0000313|Proteomes:UP000008130};
RN   [1] {ECO:0000313|EMBL:ADZ70150.1, ECO:0000313|Proteomes:UP000008130}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 25793 / CGMCC 1.9160 / SL003B-26A1
RC   {ECO:0000313|Proteomes:UP000008130}, and SL003B-26A1
RC   {ECO:0000313|EMBL:ADZ70150.1};
RX   PubMed=21478361; DOI=10.1128/JB.00333-11;
RA   Li S.G., Tang Y.Q., Nie Y., Cai M., Wu X.L.;
RT   "Complete genome sequence of Polymorphum gilvum SL003B-26A1T, a crude oil-
RT   degrading bacterium from oil-polluted saline soil.";
RL   J. Bacteriol. 193:2894-2895(2011).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {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|ARBA:ARBA00007249, ECO:0000256|HAMAP-
CC       Rule:MF_00118}.
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DR   EMBL; CP002568; ADZ70150.1; -; Genomic_DNA.
DR   EMBL; CP002568; ADZ70163.1; -; Genomic_DNA.
DR   RefSeq; WP_013652468.1; NC_015259.1.
DR   AlphaFoldDB; F2J5R7; -.
DR   STRING; 991905.SL003B_1723; -.
DR   KEGG; pgv:SL003B_1723; -.
DR   KEGG; pgv:SL003B_1737; -.
DR   PATRIC; fig|991905.3.peg.1766; -.
DR   eggNOG; COG0050; Bacteria.
DR   HOGENOM; CLU_007265_0_0_5; -.
DR   OMA; EGDKEWG; -.
DR   OrthoDB; 9803139at2; -.
DR   Proteomes; UP000008130; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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   CDD; cd03707; EFTU_III; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
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   NCBIfam; TIGR00485; EF-Tu; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
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; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00118}; Reference proteome {ECO:0000313|Proteomes:UP000008130}.
FT   DOMAIN          10..206
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT   BINDING         81..85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT   BINDING         136..139
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   396 AA;  43047 MW;  3CA41541106EE42A CRC64;
     MAKEKFERTK PHVNIGTIGH VDHGKTTLTA AITMTLAETG GAVAKAYDQI DAAPEEKARG
     ITISTAHVEY ETENRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI
     LLARQVGVPA LVVFMNKVDQ VDDEELLELV EMELRELLSS YDFPGDDIPI VKGSALAAVE
     NRDPAIGRDA IRALMAAVDE YIPTPERPID QPFLMPIEDV FSISGRGTVV TGRVERGIVK
     VGEEVEIVGI RDTRKTTVTG VEMFRKLLDQ GQAGDNIGAL IRGIGREDVE RGQVLCKPGS
     VTPHTKFKAE AYILTKEEGG RHTPFFTNYR PQFYFRTTDV TGIVSLPEGT EMVMPGDNVS
     VEVELIVPIA MEEGLRFAIR EGGRTVGAGV VASIIK
//
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