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Database: UniProt
Entry: R5USL2_9FIRM
LinkDB: R5USL2_9FIRM
Original site: R5USL2_9FIRM 
ID   R5USL2_9FIRM            Unreviewed;       900 AA.
AC   R5USL2;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Translation elongation factor G {ECO:0000313|EMBL:CCZ78719.1};
GN   ORFNames=BN518_02245 {ECO:0000313|EMBL:CCZ78719.1};
OS   Roseburia sp. CAG:18.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX   NCBI_TaxID=1262941 {ECO:0000313|EMBL:CCZ78719.1, ECO:0000313|Proteomes:UP000018230};
RN   [1] {ECO:0000313|EMBL:CCZ78719.1, ECO:0000313|Proteomes:UP000018230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:18 {ECO:0000313|Proteomes:UP000018230};
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:CCZ78719.1}.
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DR   EMBL; CBAP010000116; CCZ78719.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5USL2; -.
DR   Proteomes; UP000018230; 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   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   CDD; cd10912; PIN_YacP-like; 1.
DR   CDD; cd03711; Tet_C; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.240; -; 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; IPR035647; EFG_III/V.
DR   InterPro; IPR000640; EFG_V-like.
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; IPR035650; Tet_C.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   InterPro; IPR010298; YacP-like.
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; PF00679; EFG_C; 1.
DR   Pfam; PF14492; EFG_III; 1.
DR   Pfam; PF03764; EFG_IV; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF05991; NYN_YacP; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   PRINTS; PR01037; TCRTETOQM.
DR   SMART; SM00838; EFG_C; 1.
DR   SMART; SM00889; EFG_IV; 1.
DR   SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
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   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   Elongation factor {ECO:0000313|EMBL:CCZ78719.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018230}.
FT   DOMAIN          7..243
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          665..695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   900 AA;  100906 MW;  6AC6934882ADEB94 CRC64;
     MSRKNPAKNI NIGLLAHVDA GKTTLSEALL YATGQIRALG RVDHQDAFLD TDAQERARGI
     TIFSKQARFR LQMTDENLHS ESSVGITILD TPGHVDFSAE MERTLQVLDY AILVISGTDG
     VQGHTRTLWR LLRHYHIPTF LFVNKMDLPG ADKEAVQQQL KTELSDGCVD FTQDSGEAFF
     EEAAMGSEAL LDEYMEQGSI AEEHLAHAVA NRDLFPCYYG SALKVEGVKE LLAGFAKYHR
     APEYEDEFSA RVYKIGRDTK GARLTYLKVT GGTLHVKDRI SYDGLEEKVD QIRLYSGEKF
     ETAEAVEAGE VCAVTGLTTT VPGQGLGAQQ ESSVPVLEPV LNYRIYLPDE VNAVEMMEKL
     KQLEEEDPQL HILWNEQLQE IHAQMMGQVQ IEVLTQLIKE RFGVVVVFGQ GNIVYKETIA
     KPVEGVGHFE PLRHYAEVHL LLEPGEPGSG IEVASACSED VLDLNWQRLI ATHIMEREHP
     GVLTGSALTD VKITILSGRA HIKHTEGGDF RQATYRAIRQ GLKSTESVLL EPVYAFTLEV
     PQEMVGRAMT DLKQRAGKFD SPEFGTGNGM DYAVLQGTVP VATMQDYSSE VHAYTRGLGH
     LTLELSGYDV CHNSEEVIAG IGYDSEADTA NPTGSVFCAH GAGFIVPWDQ VDDYMHLPQQ
     FVPEEETQTP TDGRSYETDG QSFGPVHRQQ SSGKTGWELD QELQQIYARE FGMSREDMED
     QERRKWLKKK SDAPKPNVVK YDKKGNPIYP AKEPQEEYLI VDGYNIIFAW KDLNELSRVN
     IDSARDKLLD ILSNYQGYKS CPVLVVFDAY KRKEHPGAKS KYHNLDVVYT KTDETADAFI
     ERTVHEIGHK YRVTVATNDG LEQLTVMSQG ALRMSADNLR EEIERLSRLE YENYLASQKR
//
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