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Database: UniProt
Entry: J7T9X4_9FIRM
LinkDB: J7T9X4_9FIRM
Original site: J7T9X4_9FIRM 
ID   J7T9X4_9FIRM            Unreviewed;       639 AA.
AC   J7T9X4;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Tetracycline resistance protein TetM {ECO:0000313|EMBL:EJO23765.1};
GN   Name=tetM {ECO:0000313|EMBL:EJO23765.1};
GN   ORFNames=HMPREF1148_2125 {ECO:0000313|EMBL:EJO23765.1};
OS   Selenomonas sp. FOBRC6.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Selenomonas.
OX   NCBI_TaxID=936572 {ECO:0000313|EMBL:EJO23765.1, ECO:0000313|Proteomes:UP000006984};
RN   [1] {ECO:0000313|EMBL:EJO23765.1, ECO:0000313|Proteomes:UP000006984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FOBRC6 {ECO:0000313|EMBL:EJO23765.1,
RC   ECO:0000313|Proteomes:UP000006984};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (JUL-2012) 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:EJO23765.1}.
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DR   EMBL; ALKG01000006; EJO23765.1; -; Genomic_DNA.
DR   RefSeq; WP_002602099.1; NZ_ALKG01000006.1.
DR   AlphaFoldDB; J7T9X4; -.
DR   SMR; J7T9X4; -.
DR   STRING; 936572.HMPREF1148_2125; -.
DR   GeneID; 85010053; -.
DR   PATRIC; fig|936572.3.peg.70; -.
DR   eggNOG; COG0480; Bacteria.
DR   Proteomes; UP000006984; 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; 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; 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   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          1..242
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   639 AA;  72354 MW;  DB446D1AF93D8F58 CRC64;
     MKIINIGILA HVDAGKTTLT ESLLYTSGAI AEQGNVDKGT TRTDTMILER QRGITIQTAV
     TSFCWNDYKI NIVDTPGHMD FLTEAYRSLS VLDGAVLVIS AKDGVQAQTR ILFHALQKMD
     IPTIIFINKI DQNGIDLRRV YQSIKDKLTS DMIVMQEVSL SPKITMTDIS DLDKWDMIIS
     GSDELLERYV AEDSLDIQEL QYEKCKRTRC CSLFPVYHGS AKDNLGTEKL IEAITETFIT
     ETDDIQSELC GYVFKVEYTE RKKRLSYLRL YHGTLHLRDT LLLSKKEKIK ITEMCIPSNG
     EIVPVDHACP GEIVILADDT LKLNDILGNE KLLPHKTRID NPMPLLRTTV EPQKPEQREA
     LLNALTEIAD TDPLLHFDID TVTHEIILSF LGKVQLEVIC SLLEEKYHVG VAMKEPSVIY
     LERPQKKASY TIHIEVPPNP FWASIGLTVT PLPVGSGTQY KSEVSLGYLN QSFQNAVMEG
     VRYGMEQGLY GWGVTDCQIC FDYGVYYSPV STPADFRFLA PVVLEQALKK AGTQLLEPYL
     SFTLFAPQEY LSRAYNDAPK YCAIIESTRL EKDEVIFKGE IPARCIGEYR NDLNFYTNGR
     SVCITELKGY QETSGEPVFQ PRRPNSRLDK IRHMFQKIM
//
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