ID G9A4S8_RHIFH Unreviewed; 391 AA.
AC G9A4S8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 13-SEP-2023, entry version 60.
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=tufa3 {ECO:0000313|EMBL:CCE95572.1};
GN Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118}, tufa1
GN {ECO:0000313|EMBL:CCE95558.1};
GN OrderedLocusNames=SFHH103_01059 {ECO:0000313|EMBL:CCE95558.1},
GN SFHH103_01073 {ECO:0000313|EMBL:CCE95572.1};
OS Rhizobium fredii (strain HH103) (Sinorhizobium fredii).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=1117943 {ECO:0000313|EMBL:CCE95572.1, ECO:0000313|Proteomes:UP000007735};
RN [1] {ECO:0000313|EMBL:CCE95572.1, ECO:0000313|Proteomes:UP000007735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH103 {ECO:0000313|EMBL:CCE95572.1,
RC ECO:0000313|Proteomes:UP000007735};
RX PubMed=22374952; DOI=10.1128/JB.06729-11;
RA Weidner S., Becker A., Bonilla I., Jaenicke S., Lloret J., Margaret I.,
RA Puhler A., Ruiz-Sainz J.E., Schneiker-Bekel S., Szczepanowski R.,
RA Vinardell J.M., Zehner S., Gottfert M.;
RT "Genome sequence of the soybean symbiont Sinorhizobium fredii HH103.";
RL J. Bacteriol. 194:1617-1618(2012).
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; HE616890; CCE95558.1; -; Genomic_DNA.
DR EMBL; HE616890; CCE95572.1; -; Genomic_DNA.
DR RefSeq; WP_012707739.1; NC_016812.1.
DR AlphaFoldDB; G9A4S8; -.
DR STRING; 1117943.SFHH103_01059; -.
DR GeneID; 48972679; -.
DR KEGG; sfh:SFHH103_01059; -.
DR KEGG; sfh:SFHH103_01073; -.
DR PATRIC; fig|380.5.peg.1129; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_1_5; -.
DR OMA; EGDKEWG; -.
DR Proteomes; UP000007735; 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}; Hydrolase {ECO:0000313|EMBL:CCE95572.1};
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}.
FT DOMAIN 10..201
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 76..80
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT BINDING 131..134
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ SEQUENCE 391 AA; 42663 MW; 65D5D3E550C50658 CRC64;
MAKSKFERNK PHVNIGTIGH VDHGKTSLTA AITKYFGEFK AYDQIDAAPE EKARGITIST
AHVEYETPAR HYAHVDCPGH ADYVKNMITG AAQMDGAILV VSAADGPMPQ TREHILLARQ
VGVPAIVVFL NKVDQVDDAE LLELVELEVR ELLSSYEFPG DDIPIVKGSA LAALEDSDKK
IGEDAIRELM AAVDAYIPTP ERPVDLPFLM PIEDVFSISG RGTVVTGRVE RGIVKVGEEI
EIVGIRPTTK TTCTGVEMFR KLLDQGQAGD NIGALLRGVD RNGVERGQVL CKPGSVKPHR
KFKAEAYILT KEEGGRHTPF FTNYRPQFYF RTTDVTGIVT LPEGTEMVMP GDNVTVDVEL
IVPIAMEEKL RFAIREGGRT VGAGIVASIV E
//