ID R5P8K5_9BACT Unreviewed; 570 AA.
AC R5P8K5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Elongation factor G {ECO:0000313|EMBL:CCZ12810.1};
GN ORFNames=BN465_02042 {ECO:0000313|EMBL:CCZ12810.1};
OS Prevotella sp. CAG:1092.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262919 {ECO:0000313|EMBL:CCZ12810.1, ECO:0000313|Proteomes:UP000017987};
RN [1] {ECO:0000313|EMBL:CCZ12810.1, ECO:0000313|Proteomes:UP000017987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:1092 {ECO:0000313|Proteomes:UP000017987};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCZ12810.1}.
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DR EMBL; CAZL010000383; CCZ12810.1; -; Genomic_DNA.
DR AlphaFoldDB; R5P8K5; -.
DR STRING; 1262919.BN465_02042; -.
DR Proteomes; UP000017987; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR CDD; cd01886; EF-G; 1.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd04088; EFG_mtEFG_II; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR009022; EFG_III.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR004540; Transl_elong_EFG/EF2.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR NCBIfam; TIGR00484; EF-G; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43261:SF1; RIBOSOME-RELEASING FACTOR 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43261; TRANSLATION ELONGATION FACTOR G-RELATED; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Elongation factor {ECO:0000313|EMBL:CCZ12810.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:CCZ12810.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017987}.
FT DOMAIN 7..286
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 289..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 570 AA; 63381 MW; 37F1EB3C5879B14A CRC64;
MATRDLHLTR NIGIMAHIDA GKTTTSERIL FYTGKTHKIG EVHDGAATMD WMAQEQERGI
TITSAATTCN WNYKGNSYKI NLIDTPGHVD FTAEVERSLR VLDGAVATYS AADGVQPQSE
TVWRQADKYN VPRIGYVNKM DRSGADFFET VQQMKDILGA NPCPIQIPIG AEENFKGLVD
LIKMKAILWH DETMGAEYDV EDIPADLVDE AQEWRDKMLE NAANFDDELA ELYLEGEEVP
EDMLIAAIRK GTISMELTPM LLGSSYKNKG VQPLLDYVCA FLPSPLDTEN IVGTNPDTDE
EEDRKPSEDE PTSALAFKIA TDPFMGRLVF FRVYSGKVVA GSYVYNPRSR KKERISRLFQ
MNSNKEIPME TIDAGDIGAG VGFKDIRTGD TLCDENNPIV LESMTFPDTV ISIAVEPKSQ
ADIAKLDNGL AKLAEEDPTF TVRTDEQSGQ TIISGMGELH LDIIIDRLKR EFKVECNQGK
PQVNYKEAIL GTAQSRETYK KQSGGRGKFA CIDVTIGPKD EDYKEDDLQF INEVKGGNIP
KEFIPSVEKG FVRPLSLVWV SFTSISLSTV
//
