ID A4H279_STRPY Unreviewed; 639 AA.
AC A4H279;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Tetracycline resistance protein {ECO:0000313|EMBL:CAL69903.1};
GN Name=tet(M) {ECO:0000313|EMBL:CAL69903.1};
OS Streptococcus pyogenes.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1314 {ECO:0000313|EMBL:CAL69903.1};
RN [1] {ECO:0000313|EMBL:CAL69903.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C-105 {ECO:0000313|EMBL:CAL69903.1};
RX PubMed=17261630; DOI=10.1128/AAC.01484-06;
RA Brenciani A., Bacciaglia A., Vecchi M., Vitali L.A., Varaldo P.E.,
RA Giovanetti E.;
RT "Genetic elements carrying erm(B) in Streptococcus pyogenes and association
RT with tet(M) tetracycline resistance gene.";
RL Antimicrob. Agents Chemother. 51:1209-1216(2007).
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; AM411624; CAL69903.1; -; Genomic_DNA.
DR RefSeq; WP_063856401.1; NG_048245.1.
DR AlphaFoldDB; A4H279; -.
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; 72488 MW; B9275A3FD891742B CRC64;
MKIINIGVLA HVDAGKTTLT ESLLYTSGAI TELGSVDKGT TRTDNTLLER QRGITIQTGI
TSFQWENTKV NIIDTPGHMD FLAEVYRSLS VLDGAILLIS AKDGVQAQTR ILFHALRKMG
IPTIFFINKI DQNGIDLSTV YQDIKEKLSA EIVIKQKVEL YPNMCVTNFT ESEQWDTVIE
GNDDLLEKYM SGKSLEALEL QQEESIRFHN CSLFPVYYGS AKNNIGIDNL IEVITNKFYS
STHRGPSELC GNVFKIEYSE KRQRLAYIRL YSGVLHLRDS VRISEKEKIK ITEMYTSING
ELCKIDKAYS GEIVILQNEF LKLNSVLGDT KLLPQRERIE NPLPLLQTTV EPSKPQQREM
LLDALLEISD SDPLLRYYVD SATHEIILSF LGKVQMEVTC ALLQEKYHVE IEIKEPTVIY
MERPLKKAEY TIHIEVPPNP FWASIGLSVA PLPLGSGVQY ESSVSLGYLN QSFQNAVMEG
IRYGCEQGLY GWNVTDCKIC FKYGLYYSPV STPADFRMLA PIVLEQVLKK AGTELLEPYL
SFKIYAPQEY LSRAYNDAPK YCANIVDTQL KNNEVILSGE IPARCIQEYR SDLTFFTNGR
SVCLTELKGY HVTTGEPVCQ PRRPNSRIDK VRYMFNKIT
//
