ID G2IF77_9CLOT Unreviewed; 397 AA.
AC G2IF77;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 63.
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:BAK81801.1};
GN ORFNames=RATSFB_1227 {ECO:0000313|EMBL:BAK81789.1}, RATSFB_1239
GN {ECO:0000313|EMBL:BAK81801.1};
OS Candidatus Arthromitus sp. SFB-rat-Yit.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Candidatus Arthromitus.
OX NCBI_TaxID=1041504 {ECO:0000313|EMBL:BAK81801.1, ECO:0000313|Proteomes:UP000001273};
RN [1] {ECO:0000313|EMBL:BAK81801.1, ECO:0000313|Proteomes:UP000001273}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SFB-rat-Yit {ECO:0000313|EMBL:BAK81801.1};
RX PubMed=21925114;
RA Prakash T., Oshima K., Morita H., Fukuda S., Imaoka A., Kumar N.,
RA Sharma V.K., Kim S.-W., Takahashi M., Saitou N., Taylor T.D., Ohno H.,
RA Umesaki Y., Hattori M.;
RT "Complete genome sequences of rat and mouse segmented filamentous bacteria,
RT a potent inducer of th17 cell differentiation.";
RL Cell Host Microbe 10:273-284(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; AP012210; BAK81789.1; -; Genomic_DNA.
DR EMBL; AP012210; BAK81801.1; -; Genomic_DNA.
DR RefSeq; WP_014095247.1; NC_016012.1.
DR AlphaFoldDB; G2IF77; -.
DR STRING; 1041504.RATSFB_1227; -.
DR KEGG; asb:RATSFB_1227; -.
DR KEGG; asb:RATSFB_1239; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_0_9; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000001273; 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; 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}.
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 397 AA; 43786 MW; 5E793D1001B52DBC CRC64;
MSKAKFERNK PHVNIGTIGH VDHGKTTLTA AITTVLANKG YAEAFKYDEI DKAPEEKERG
ITINTAHVEY ETDGRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
LLASRVGVDY IVVFLNKADM VDDEELLELV EMEVRDLLNE YKFPGDDTPI IKGSALRALE
NPTDSEATAC IMELMDAVDS YIPTPERATD KPFLMPVEDV FTITGRGTVA TGRVETGILK
VQEEVEIIGL KEEKSKTVIT GIEMFRKLLD EAQAGDNIGA LLRGIQRSDI ERGQVLAKPG
TVNPHTNFIG QVYVLKKEEG GRHKPFFDGY RPQFYFRTTD VTGNIKLPEG KEMVMPGDHI
DMEVELITPI AMDEGLRFAI REGGRTVGSG VVSKINK
//
