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Database: UniProt
Entry: A0A255SD26_9BACT
LinkDB: A0A255SD26_9BACT
Original site: A0A255SD26_9BACT 
ID   A0A255SD26_9BACT        Unreviewed;       719 AA.
AC   A0A255SD26;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Tetracycline resistance protein TetQ {ECO:0000256|ARBA:ARBA00013902};
GN   ORFNames=CIK97_04320 {ECO:0000313|EMBL:OYP50919.1};
OS   Prevotella sp. P3-120.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=2024220 {ECO:0000313|EMBL:OYP50919.1, ECO:0000313|Proteomes:UP000216094};
RN   [1] {ECO:0000313|EMBL:OYP50919.1, ECO:0000313|Proteomes:UP000216094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P3-120 {ECO:0000313|EMBL:OYP50919.1,
RC   ECO:0000313|Proteomes:UP000216094};
RA   Accetto T., Nograsek B., Avgustin G.;
RT   "Comparative genomics of non-oral Prevotella species.";
RL   Submitted (AUG-2017) 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:OYP50919.1}.
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DR   EMBL; NPJD01000026; OYP50919.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A255SD26; -.
DR   Proteomes; UP000216094; 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   PRINTS; PR00315; ELONGATNFCT.
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:OYP50919.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:OYP50919.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216094}.
FT   DOMAIN          7..281
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   719 AA;  80255 MW;  E43F7340E4E16B05 CRC64;
     MKVYQTNEIK NIALLGSAGS GKTTLAESML FEAGIIKRRG TVEQKNTVSD YFPVEQEYGY
     SVFSTVFHVE WNNKKLNIID CPGSDDFVGG AITALNVTDQ AVILINGQYG PEVGTQNAFR
     YTDKLNKPVI FLINQLDREH CDFDSLLANM KEIYGDKCVP VQYPIATGPG FNAVIDVLLM
     KKYSWNPEGG APTIEDIPAE EMDKAKEMHA ALVEAAAAND DTLMEKFFES ESLTEDEMRE
     GIRKGLVTRS IFPVFCVCAG KDMGVRRLME FLGNVVPFVS EMPKLHNTRG EEISPDTAGP
     TSIYFFKTGM EPHIGEVSYF KVMSGTLKAG ADLQNADRGS KERIAQIYAC AGANRIAVDE
     MHAGDIGCTV KLKDVKTGNT LNDKDTDNRF DFIKYPNPKY SRAVKAINEA ETEKMMAALT
     KMRQEDPTWV VEQSKELRQI IVRGQGEFHL RTLKWRMENN EKIKIEYIEP KIPYRETITK
     AARADYRHKK QSGGAGQFGE VHMIVEPYAD GMPAPTVFKF GGQEYRINVK NQEVVDLEWG
     GKLVFINSVV GGAIDARFMP AILKGVMERM ERGPLTGSYA RDVRVIVYDG KMHPVDSNEL
     SFMLAARNAF SAAFREAGPK VLEPIYDLEV YVPADYMGDV MSDLQGRRAL IMGMDSEAGY
     QKLSAKIPLK ELSNYSIALS SITGGRASFT TKFASYELVP NEIQQQLIQQ HEAETKEEE
//
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