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Database: UniProt
Entry: A0A3N2NJ23_9BACT
LinkDB: A0A3N2NJ23_9BACT
Original site: A0A3N2NJ23_9BACT 
ID   A0A3N2NJ23_9BACT        Unreviewed;       718 AA.
AC   A0A3N2NJ23;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Tetracycline resistance protein TetQ {ECO:0000256|ARBA:ARBA00013902};
GN   ORFNames=EEL53_05160 {ECO:0000313|EMBL:ROT22425.1};
OS   Muribaculaceae bacterium Isolate-114 (HZI).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae.
OX   NCBI_TaxID=2486475 {ECO:0000313|EMBL:ROT22425.1, ECO:0000313|Proteomes:UP000273368};
RN   [1] {ECO:0000313|EMBL:ROT22425.1, ECO:0000313|Proteomes:UP000273368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate-114 (HZI) {ECO:0000313|Proteomes:UP000273368};
RA   Clavel T., Strowig T.;
RT   "Sequence and cultivation study of Muribaculaceae reveals novel species,
RT   host preference, and functional potential of this yet undescribed family.";
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   -!- 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:ROT22425.1}.
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DR   EMBL; RIBN01000006; ROT22425.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N2NJ23; -.
DR   Proteomes; UP000273368; 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; cd04170; EF-G_bact; 1.
DR   CDD; cd01434; EFG_mtEFG1_IV; 1.
DR   CDD; cd03713; EFG_mtEFG_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; IPR047872; EFG_IV.
DR   InterPro; IPR035649; EFG_V.
DR   InterPro; IPR000640; EFG_V-like.
DR   InterPro; IPR004161; EFTu-like_2.
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; IPR005517; Transl_elong_EFG/EF2_IV.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43261:SF7; ELONGATION FACTOR G-LIKE PROTEIN; 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; 2.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
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; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   Elongation factor {ECO:0000313|EMBL:ROT22425.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:ROT22425.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000273368}.
FT   DOMAIN          7..286
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   718 AA;  80155 MW;  764F01067D6CFEBF CRC64;
     MKIYKTNEIK NIALLGSKGA GKTTLAESMI FECGVIKRRG TIEAKNTVSD YFPVEKEYGY
     SVFSTVFNAE FNGKKLNIID CPGADDFVGN AYTALGVCDM GLILVDAQYG VEVGTENIFR
     TTAKLKKPVI FGLNQMDGEK ADFENVMEQM REHFGPRVVQ IQYPLESGPN FHSMIDVLLM
     KKYEWGPEGG TPVISEIPED QLEKARELNQ KLVEAAAEND ETLMEKFFEQ GSLTEDEMRE
     GIRKGLIDRS IYPVVVLSAA KDMGVRRLME FLGNVCPFVS DMPAPETVAG EEVKPDAEGP
     LSVFFFKTSV EPHIGEVSYF KVMSGTLKAG EDLENVSRGG KERLAQIFTV CGQLRNPIET
     LEAGDIGAAV KLKDVRTGNT LDAKGCDYQF NFIKYPQPKY TRAIRPVTES DAEKLAGILT
     RMHEEDPTWI VEQSKELKQT LVKGQGEFHL RTLKWRIENN EKLPIEFIDQ KIPYRETITK
     AARADYRHKK QSGGSGQFGE VHLIIEPYTE GMPEPDTYKF GNQEFKLNVR DKQEIPLEWG
     GKLVVYNCIV GGAIDARFIP AIVKGLMDRM EQGPLTGSYA RDVRVMIYDG KMHPVDSNEI
     SFRLAGRNAF SQAFKAANPK ILEPVYDVEV LTPGDTMGDV MSDLQGRRAL IMGMASENGI
     EKLSAKVPLK EMASYSTSLS SITGGRSSFT MEFSSYELVP SDVQEKLLKE YAETQTED
//
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