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Database: UniProt
Entry: A0A3G9JJD1_9FIRM
LinkDB: A0A3G9JJD1_9FIRM
Original site: A0A3G9JJD1_9FIRM 
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}.
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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
//
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