ID A0A3G9JJD1_9FIRM Unreviewed; 647 AA.
AC A0A3G9JJD1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Tetracycline resistance ribosomal protection protein Tet(O) {ECO:0000313|EMBL:BBH25103.1};
GN Name=tetO {ECO:0000313|EMBL:BBH25103.1};
GN ORFNames=SG0102_00370 {ECO:0000313|EMBL:BBH25103.1};
OS Intestinibaculum porci.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Intestinibaculum.
OX NCBI_TaxID=2487118 {ECO:0000313|EMBL:BBH25103.1, ECO:0000313|Proteomes:UP000268059};
RN [1] {ECO:0000313|EMBL:BBH25103.1, ECO:0000313|Proteomes:UP000268059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG0102 {ECO:0000313|EMBL:BBH25103.1,
RC ECO:0000313|Proteomes:UP000268059};
RA Kim J.S., Choe H., Lee Y.R., Kim K.M., Park D.S.;
RT "Novel Erysipelotrichaceae bacterium isolated from small intestine of a
RT swine.";
RL Submitted (NOV-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP019309; BBH25103.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G9JJD1; -.
DR KEGG; ebm:SG0102_00370; -.
DR InParanoid; A0A3G9JJD1; -.
DR Proteomes; UP000268059; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR CDD; cd03711; Tet_C; 1.
DR CDD; cd03690; Tet_II; 1.
DR CDD; cd16258; Tet_III; 1.
DR CDD; cd01684; Tet_like_IV; 1.
DR CDD; cd04168; TetM_like; 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 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 PRINTS; PR00315; ELONGATNFCT.
DR PRINTS; PR01037; TCRTETOQM.
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 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:UP000268059}.
FT DOMAIN 9..251
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 647 AA; 72320 MW; E2A6771D78191BAB CRC64;
MKIINNNHMK IINIGILAHV DAGKTTLTES LLYASGAISE PGSVEKGTTR TDSMFLERQR
GITIQAAVTS FQWHRCKVNI VDTPGHMDFL AEVYRSLAVL DGAILVISAK DGVQAQTRIL
FHALRKMSIP TVIFINKIDQ AGVDLQSVVQ SVRDKLSADI IIKQTVSLSP EIVLEENTDI
EAWDAVIENN DKLLEKYIAG EPISREKLVR EEQRRVQDAS LFPVYYGSAK KGLGIQPLMD
AVTGLFQPIG EQGSAALCGS VFKVEYTDCG QRRVYLRLYS GTLRLRDTVA LAGREKLKIT
EMRIPSKGEI VRTDTAYPGE IVILPSDSVR LNDVLGDPTR LPRKRWREDP LPMLRTSIAP
KTAAQRERLL DALTQLADTD PLLRCEVDSI THEIILSFLG RVQLEVVSAL LSEKYKLETV
VKEPTVIYME RPLKAASHTI HIEVPPNPFW ASIGLSVTPL PLGSGVQYES RVSLGYLNQS
FQNAVRDGIR YGLEQGLFGW NVTDCKICFE YGLYYSPVST PADFRSLAPI VLEQALKESG
TQLLEPYLSF TLYAPQEYLS RAYHDAPKYC ATIETVQVKK DEVVFTGEIP ARCIQAYRTD
LAFYTNGQSV CLTELKGYQA AVGKPVIQPR RPNSRLDKVR YMFQKIM
//