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Database: UniProt
Entry: A0A0A2EPF1_9PORP
LinkDB: A0A0A2EPF1_9PORP
Original site: A0A0A2EPF1_9PORP 
ID   A0A0A2EPF1_9PORP        Unreviewed;       720 AA.
AC   A0A0A2EPF1;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Tetracycline resistance protein TetQ {ECO:0000256|ARBA:ARBA00013902};
GN   ORFNames=HW49_06155 {ECO:0000313|EMBL:KGN79577.1};
OS   Porphyromonadaceae bacterium COT-184 OH4590.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae.
OX   NCBI_TaxID=1517682 {ECO:0000313|EMBL:KGN79577.1, ECO:0000313|Proteomes:UP000030107};
RN   [1] {ECO:0000313|EMBL:KGN79577.1, ECO:0000313|Proteomes:UP000030107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COT-184 OH4590 {ECO:0000313|Proteomes:UP000030107};
RA   Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA   Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT   "Porphyromonadaceae COT-184_OH4590 Genome sequencing.";
RL   Submitted (AUG-2014) 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:KGN79577.1}.
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DR   EMBL; JRAN01000046; KGN79577.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2EPF1; -.
DR   eggNOG; COG0480; Bacteria.
DR   OrthoDB; 9801591at2; -.
DR   Proteomes; UP000030107; 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:KGN79577.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:KGN79577.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030107}.
FT   DOMAIN          7..280
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   720 AA;  80081 MW;  CBB19102114151B6 CRC64;
     MKIYKSSEIR NVSLLGSAGT GKTTLVEAML FESGAIKRKG TIEGKNTVSD YFPVEQEYGY
     SVLPTIITAE WANKKINIID CPGADDFVGG AITSLAVTEQ SVILVNAQYG VEVGTHNHFR
     YADKFRKPVI FAVNQLDREM ADFDKTFEQL RESFGGKVAL VQYPVNAGTA FNAVIDVLKL
     KMYRWKPEGG QPEELDIPDS EKAKAEELHA ALIEAAAEND ETLMERFFEQ GSLKEEEIFE
     GIHKGLINCG IYPVLCLCGG KSMGVRRLME FLGAVAPSPV EMTAPVTTGG VEVKPDANAP
     TSLFFFKTSV EPHIGEVLYF KVISGKIKGG DDMTNVSRNG NKERISQIFS VAGQTRTQVD
     EMVAGDIGAT VKLKDVRTGN TVNGKDVDWV FPEVNYPAPK YRRAIKAKNE GEDEKLGEIL
     NRLHAEDPTW VIERSKELRQ TILSGQGEFH LRTLKWRVEN LDKIMIEYSE PRIPYRETIT
     KAARADYRHK KQSGGAGQFG EVHLIIEPYQ EDVPAQEVYK FNGQEYKISV RDTQEIDLDW
     GGKLIFINSI VGGSIDARFM PAILKGIMDR MEQGPLTGSY ARDVRVIVYD GKMHPVDSNE
     ISFRLAGRNA FAQAFKEAGP KLLEPIYDLD VLVPSDRMGD VMSDLQGRRG MVLGMNSERG
     FEHLKAKVPL KEVSSYSTAL SSISGGRASF AMKFSSYELC PTDVQDKLIK EYEATQNDEE
//
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