ID A0A0A2GGB5_9PORP Unreviewed; 395 AA.
AC A0A0A2GGB5;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
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:KGN74151.1};
GN Synonyms=tufA {ECO:0000313|EMBL:SUB78729.1};
GN ORFNames=HQ47_05640 {ECO:0000313|EMBL:KGN74151.1}, NCTC11632_02098
GN {ECO:0000313|EMBL:SUB89966.1}, NCTC13100_01913
GN {ECO:0000313|EMBL:SUB78729.1};
OS Porphyromonas macacae.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=28115 {ECO:0000313|EMBL:KGN74151.1, ECO:0000313|Proteomes:UP000030103};
RN [1] {ECO:0000313|EMBL:KGN74151.1, ECO:0000313|Proteomes:UP000030103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-192 OH2859 {ECO:0000313|Proteomes:UP000030103}, and
RC COT-192_OH2859 {ECO:0000313|EMBL:KGN74151.1};
RA Wallis C., Deusch O., O'Flynn C., Davis I., Horsfall A., Kirkwood N.,
RA Harris S., Eisen J.A., Coil D.A., Darling A.E., Jospin G., Alexiev A.;
RT "Draft Genome Sequence of Porphyromonas macacae COT-192_OH2859.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000254156, ECO:0000313|Proteomes:UP000254263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC11632 {ECO:0000313|EMBL:SUB89966.1,
RC ECO:0000313|Proteomes:UP000254156}, and NCTC13100
RC {ECO:0000313|EMBL:SUB78729.1, ECO:0000313|Proteomes:UP000254263};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Abolishes the inhibitory effect of tetracyclin on protein
CC synthesis by a non-covalent modification of the ribosomes.
CC {ECO:0000256|ARBA:ARBA00003987}.
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; JRFA01000015; KGN74151.1; -; Genomic_DNA.
DR EMBL; UGTI01000001; SUB78729.1; -; Genomic_DNA.
DR EMBL; UGTF01000002; SUB89966.1; -; Genomic_DNA.
DR RefSeq; WP_018359871.1; NZ_UGTI01000001.1.
DR AlphaFoldDB; A0A0A2GGB5; -.
DR STRING; 28115.HQ47_05640; -.
DR eggNOG; COG0050; Bacteria.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000030103; Unassembled WGS sequence.
DR Proteomes; UP000254156; Unassembled WGS sequence.
DR Proteomes; UP000254263; Unassembled WGS sequence.
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}; Hydrolase {ECO:0000313|EMBL:KGN74151.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000030103}.
FT DOMAIN 10..204
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 395 AA; 43618 MW; C5986A4B3D03043A CRC64;
MAKEHFNRTK PHVNIGTIGH VDHGKTTLTA AITTVLAKKG LSELRSFDSI DNAPEEKERG
ITINTSHVEY ETANRHYAHV DCPGHADYVK NMVTGAAQMD GAIIVVAATD GPMPQTREHI
LLARQVNVPR LVVFMNKCDI VDDEEMLELV EMDMRELLEF YNFDGDNTPI IRGSALGALN
GDAKWEDKIM ELMDAVDTWI PLPERDVDKP FLMPVEDVFS ITGRGTVATG RIETGIVKVG
DEVQIIGLGA EGMKSVVTGV EMFRKLLDEG QAGDNVGLLL RGIDKDQIKR GMVLAHPGQV
KPHKHFKAEV YILKKEEGGR HTPFHNKYRP QFYIRTLDVT GEITLPEGTE MVMPGDNVTI
DVELIYPVAC NVGLRFAIRE GGRTVGAGQI TALED
//
