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}.
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; 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
//