ID A0A143Y0J7_9FIRM Unreviewed; 639 AA.
AC A0A143Y0J7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Tetracycline resistance protein TetO {ECO:0000313|EMBL:CVI73754.1};
GN Name=tetO_3 {ECO:0000313|EMBL:CVI73754.1};
GN ORFNames=BN3660_03320 {ECO:0000313|EMBL:CVI73754.1};
OS Eubacteriaceae bacterium CHKCI004.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae.
OX NCBI_TaxID=1780380 {ECO:0000313|EMBL:CVI73754.1, ECO:0000313|Proteomes:UP000199324};
RN [1] {ECO:0000313|EMBL:CVI73754.1, ECO:0000313|Proteomes:UP000199324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHKC4 {ECO:0000313|EMBL:CVI73754.1};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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; FCNR01000069; CVI73754.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A143Y0J7; -.
DR STRING; 1780380.BN3660_03320; -.
DR OrthoDB; 9801472at2; -.
DR Proteomes; UP000199324; 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: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; 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:UP000199324}.
FT DOMAIN 1..242
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 639 AA; 71932 MW; ED9A5BC07ECEE919 CRC64;
MKIINIGILA HVDAGKTTLT ESLLYTSGAV PELGSVDKGT TRTDTMLLER QRGITIQTAV
TSFGWKNYKI NIVDTPGHMD FLAEVYRSLA VLDGAILVVS AKDGVQAQTR VLFHALQKMK
IPTIIFVNKI DQEGIDLQSV YQNIREKLSD DVMVMQDVSL TPEVSLTDIE DIEKWDSIIA
GNDELLEKYI AGEPLKIQDL QREKCRRMQN GSLFPIYHGS AKNNIGTEKL IEVIAETFTS
GADNDQSELC GSVFKIEYTD QKKRLVYLRL YSGTLHLRDT ILLPQNQKLK ITEMRIPSNG
EIIPADTACC GEIVILTNDT LKLNDTLGNV ELLPRKAWEK NPIPLLRTTV EPQNQEQRDL
LLNALTEIAD TDPLLHYYVD TITHEIIISF LGKVQLEVVC SLLVERYHVN INVKEPTVIY
LERPLKTASY TIHIEVPPNP FWASIGLTVT PLPAGSGTRF KSKVSLGYLN QSFQNAVMEG
VRYGMEQGLY GWEVTDCEIC FDYGVYYSPV STPADFRSLA PIVLEQALKR AGTQLLEPYL
SFTLFAPQEY ISRAYNDAPK YCAVIESTLL KNDEVIFTGE IPARCIGEYR NDLNFYTNGR
SVCLTELKGY QEISGEPVLQ PRRPNSRLDK VRHMFQKIT
//
