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Database: UniProt
Entry: F3QUA3_9BACT
LinkDB: F3QUA3_9BACT
Original site: F3QUA3_9BACT 
ID   F3QUA3_9BACT            Unreviewed;       625 AA.
AC   F3QUA3;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Tetracycline resistance protein TetQ {ECO:0000256|ARBA:ARBA00013902};
DE   Flags: Fragment;
GN   ORFNames=HMPREF9442_01772 {ECO:0000313|EMBL:EGG54005.1};
OS   Paraprevotella xylaniphila YIT 11841.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Paraprevotella.
OX   NCBI_TaxID=762982 {ECO:0000313|EMBL:EGG54005.1, ECO:0000313|Proteomes:UP000005546};
RN   [1] {ECO:0000313|EMBL:EGG54005.1, ECO:0000313|Proteomes:UP000005546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIT 11841 {ECO:0000313|EMBL:EGG54005.1,
RC   ECO:0000313|Proteomes:UP000005546};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2011) 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:EGG54005.1}.
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DR   EMBL; AFBR01000047; EGG54005.1; -; Genomic_DNA.
DR   RefSeq; WP_008627130.1; NZ_GL883847.1.
DR   AlphaFoldDB; F3QUA3; -.
DR   STRING; 762982.HMPREF9442_01772; -.
DR   eggNOG; COG0480; Bacteria.
DR   HOGENOM; CLU_002794_4_2_10; -.
DR   OrthoDB; 9801472at2; -.
DR   Proteomes; UP000005546; 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   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   CDD; cd03711; Tet_C; 1.
DR   CDD; cd03690; Tet_II; 1.
DR   CDD; cd16258; Tet_III; 1.
DR   CDD; cd01684; Tet_like_IV; 1.
DR   CDD; cd04168; TetM_like; 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; IPR000640; EFG_V-like.
DR   InterPro; IPR031157; G_TR_CS.
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; IPR035650; Tet_C.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   NCBIfam; TIGR00231; small_GTP; 1.
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; PR00315; ELONGATNFCT.
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.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   Elongation factor {ECO:0000313|EMBL:EGG54005.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          1..228
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EGG54005.1"
SQ   SEQUENCE   625 AA;  70561 MW;  6C9D17C5E11C36D7 CRC64;
     TSVTENLLFA SGATEKCGRV DNGDTITDSM DIEKRRGITV RASTTSIIWN GVKCNIIDTP
     GHMDFIAEVE RTFKMLDGAV LILSAKEGIQ AQTKLLFNTL QKLQIPTIIF INKIDRAGVN
     LERLYMDIKT NLSQDVLFMQ TVVDGSVYPV CSQTYIKEEY KEFVCNHDDD ILERYLADSE
     ISPADYWNTI IALVAKAKVY PVLHGSAMFN IGINELLDAI SSFILPPASV SNRLSAYLYK
     IEHDPKGHKR SFLKIIDGSL RLRDVVRIND SEKFIKIKNL KTIYQGREIN VDEVGANDIA
     IVEDMEDFRI GDYLGAEPCL IQGLSHQNPA LKSSVRPDKP EERSKVISAL NTLWIEDPSL
     SFSINSYSDE LEISLYGLTQ KEIIQTLLEE RFSVKVHFDE VKTIYKERPV KKVNKIIQIE
     VPPNPYWATI GLTLEPLPLG AGLQIESDIS YGYLNHSFQN AVFEGIRMSC QSGLHGWEVT
     DLKVTFTQAE YYSPVSTPAD FRQLTPYVFR LALQQSGVDI LEPMLCFELQ IPQVASSKAI
     TDLQKMMSEI EDISCNNEWC HIKGKVPLNT SKDYASEVSS YTKGLGIFMV KPCGYQITKD
     GYSDNIRMNE KDKLLFMFQK SMSLK
//
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