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Database: UniProt
Entry: Q70HU5_STRMT
LinkDB: Q70HU5_STRMT
Original site: Q70HU5_STRMT 
ID   Q70HU5_STRMT            Unreviewed;       639 AA.
AC   Q70HU5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   SubName: Full=Tetracycline resistance protein {ECO:0000313|EMBL:CAE46076.1};
GN   Name=tet(M) {ECO:0000313|EMBL:CAE46076.1};
OS   Streptococcus mitis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=28037 {ECO:0000313|EMBL:CAE46076.1};
RN   [1] {ECO:0000313|EMBL:CAE46076.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=254-1 {ECO:0000313|EMBL:CAE46076.1};
RX   PubMed=15519474; DOI=10.1016/j.ijantimicag.2004.06.003;
RA   Stapleton P., Adams V., Pike R., Lucas V., Roberts G., Mullany P.,
RA   Rowbury R., Wilson M., Richards H.;
RT   "Characterisation of viridans group streptococci with different levels of
RT   Tet(M)-mediated tetracycline resistance.";
RL   Int. J. Antimicrob. Agents 24:439-443(2004).
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}.
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DR   EMBL; AJ580977; CAE46076.1; -; Genomic_DNA.
DR   RefSeq; WP_063856391.1; NG_048227.1.
DR   AlphaFoldDB; Q70HU5; -.
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   Cyclin {ECO:0000313|EMBL:CAE46076.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          1..242
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   639 AA;  72566 MW;  C9847CD6CF27B844 CRC64;
     MKIINIGVLA HVDAGKTTLT ESLLYNSGAI TELGSVDKGT TRTDNTLLER QRGITIQTGI
     TSFQWENTKV NIIDTPGHMD FLAEVYRSLS VLDGAILLIS AKDGVQAQTR ILFHALRKMG
     IPTIFFINKI DQNGIDLSTV YQDIKEKLSA EIVIKQKVEL YPNMCVTNFT ESEQWDTVIE
     GNDDLLEKYM SGKSLEALEL EQEESIRFHN CSLFPVYHGS AKNNIGIDNL IEVITNKFYS
     STHRGQSELC GNVFKIEYSE KRQRLAYIRL YSGVLHLRDS VRISEREKIK ITEMYTSING
     ELCKIDKAYS GEIVILQNEF LKLNSVLGDT KLLPQRERIE NPLPLLQTTV EPSKPQQREM
     LLDALLEISD SDPLLRYYVD SATHEIILSF LGKVQMEVTC ALLQEKYHVE IEIKEPTVIY
     MERPLKKAEY TIHIEVPPNP FWASIGLSVA QLPLGSGVQY ESSVSLGYLN QSFQNAVMEG
     IRYGCEQGLY GWNVTDCKIC FKYGLYYSPV STPADFRMLA PIVLEQVLKK AGTELLEPYL
     SFKIYAPQEY LSRAYNDAPK YCANIVDTQL KNNEVILSGE IPARCIQEYR SDLTFFTNGR
     SVCLTELKGY HVTTGEPVCQ PRRPNSRIDK VRYMFNKIT
//
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