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Database: UniProt
Entry: A0A399SXF1_9BACT
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ID   A0A399SXF1_9BACT        Unreviewed;       717 AA.
AC   A0A399SXF1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Tetracycline resistance protein TetQ {ECO:0000256|ARBA:ARBA00013902};
GN   ORFNames=D1614_17265 {ECO:0000313|EMBL:RIJ46905.1};
OS   Maribellus luteus.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC   Maribellus.
OX   NCBI_TaxID=2305463 {ECO:0000313|EMBL:RIJ46905.1, ECO:0000313|Proteomes:UP000265926};
RN   [1] {ECO:0000313|EMBL:RIJ46905.1, ECO:0000313|Proteomes:UP000265926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XSD2 {ECO:0000313|EMBL:RIJ46905.1,
RC   ECO:0000313|Proteomes:UP000265926};
RA   Zhou L.Y.;
RT   "Pallidiluteibacterium maritimus gen. nov., sp. nov., isolated from coastal
RT   sediment.";
RL   Submitted (AUG-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:RIJ46905.1}.
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DR   EMBL; QWGR01000011; RIJ46905.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A399SXF1; -.
DR   OrthoDB; 9801591at2; -.
DR   Proteomes; UP000265926; 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   CDD; cd04088; EFG_mtEFG_II; 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:RIJ46905.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:RIJ46905.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265926}.
FT   DOMAIN          7..279
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   717 AA;  79485 MW;  842A4D1AA6E4AFC1 CRC64;
     MKVYKTEEIR NIALLGNAGS GKTTLAEAML FEGGVISRRG EVTSKNTVSD YNQIEQDYGN
     SVFSTLLYTE FNGKKINIID TPGMDELCGG VVSALSVTAL GLLTINTTSG IEAGTEAAIR
     HASKAHTPLI LVFNQLDHDN SNYENTLEEC KNIFGGKTTI VQYPVDAGPN FSSIIDVLKM
     KMYKYSKDGK VEVLDIPDSE KDRADELHNE LVEKAAENEE ALMELYFDKG SLTEDEMRKG
     IKLGMLARSL YPVFCTTAKK GIGVARLMEF ITNIAPAPYE KKLRPIIKGK EVKMDAADSP
     SLFVFKTSVE PHVGEITFFK VMSGTVKEGM DLVNSKSGNK ERLSQVFVSA GKNREKVDEL
     VAGDIGCTVK LKETKYNHTL SLKEAGTVFE PIQFPTPRHT VAVKAVNDSD DEKVGEVLNK
     IKYEDPTFVV EYSKELKQLL VHGQGEYHMN VLKWYFDTIH KIEVNYLAPR IPYRETITKP
     AQADYRHKKQ SGGAGQFGEV HLIIEPYNEG AAPKSMFKFG DKEQKLSVRA VEEHKLSWGG
     KLVFANCIVG GSIDARFLPA ILKGIMEKME EGPLTGSYAR DIIVYVYDGK MHPVDSNEIS
     FKLAGRNAFS MAFKNAAPKI LEPIYNLEVW VPSDRMGDAM SDLQGRRAMI MGMGSEHGME
     KISAKVPLKE MNKYTTSLSS ITGGRGVFAI AFDGYEKVPA DVQDELLKAY EAEQEEE
//
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