ID A0A1Q3L398_9BACT Unreviewed; 539 AA.
AC A0A1Q3L398;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Tetracycline resistance protein TetQ {ECO:0000256|ARBA:ARBA00013902};
GN ORFNames=BGN96_02840 {ECO:0000313|EMBL:OJU39843.1};
OS Bacteroidales bacterium 45-6.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX NCBI_TaxID=1895719 {ECO:0000313|EMBL:OJU39843.1, ECO:0000313|Proteomes:UP000185892};
RN [1] {ECO:0000313|EMBL:OJU39843.1, ECO:0000313|Proteomes:UP000185892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=45-6 {ECO:0000313|EMBL:OJU39843.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:OJU39843.1}.
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DR EMBL; MKRS01000746; OJU39843.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3L398; -.
DR Proteomes; UP000185892; 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 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; 3.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
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 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; PR01037; TCRTETOQM.
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.
PE 4: Predicted;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 318..433
FT /note="Translation elongation factor EFG/EF2"
FT /evidence="ECO:0000259|SMART:SM00889"
FT DOMAIN 435..522
FT /note="Elongation factor EFG"
FT /evidence="ECO:0000259|SMART:SM00838"
SQ SEQUENCE 539 AA; 60123 MW; E02B98C0D3CF3B30 CRC64;
MKTINIGILA HIDAGKTSIT ENLLFASGAT EVRGSVDKGN TTTDSMDLSK DILLMQSVDG
KILTSSCTIH NISEKDRETI LEKDDSLLEK YLSDTQLSNS DYWSSMIHLV QFAKLHPIYH
GSAMYGIGIE DLLNSITTFI ETSLPQENDL SAYVYKIEHN KKEQKRAYLK IIGGSLRTRK
SYNLNGSDEN LKIRSLKTFY AGNEIDVDEV STNDIAILDH AESLMVGDYL GTMPSLFDKL
NIPSPAFKSS IHPAKVEDRS KLISAMNVLS VEDPSLTFGI NADNNELEVS LYGATQREVI
LTLLEERFSV DAYFEEVKTI YKERLKTKSE YTIHIEVPPN PYWASIGLII EPLPIGAGLT
IESDISLGYL NQSFQNAVFD GVKKACESGL YGWEVTDLKV TFSHGIYYSP VSTPADFRSL
APYVFRLALQ QADVELLEPI LDFKLQIPIA VNARAITDIN KMQGEISTIT SDGDWTTILG
EIPLDTSKEY SAEVSSYTQG LGIFVTRFSG YQITNKKVSR SVELNEKDKL MYMFEKELG
//
