ID TETP_CLOPF Reviewed; 652 AA.
AC Q46306;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=Tetracycline resistance protein TetP;
DE AltName: Full=TetB(P);
GN Name=tetP; Synonyms=tetB(P);
OS Clostridium perfringens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1502;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CW92;
RX PubMed=8170402; DOI=10.1111/j.1365-2958.1994.tb00320.x;
RA Sloan J., McMurry L.M., Lyras D., Levy S.B., Rood J.I.;
RT "The Clostridium perfringens Tet P determinant comprises two overlapping
RT genes: tetA(P), which mediates active tetracycline efflux, and tetB(P),
RT which is related to the ribosomal protection family of tetracycline-
RT resistance determinants.";
RL Mol. Microbiol. 11:403-415(1994).
CC -!- FUNCTION: Abolishes the inhibitory effect of tetracyclin on protein
CC synthesis by a non-covalent modification of the ribosomes.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. TetM/TetO
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; L20800; AAA20117.1; -; Unassigned_DNA.
DR PIR; S41522; S41522.
DR RefSeq; WP_012478245.1; NG_048319.1.
DR RefSeq; YP_001967743.1; NC_010937.1.
DR AlphaFoldDB; Q46306; -.
DR SMR; Q46306; -.
DR KEGG; ag:AAA20117; -.
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; 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 3: Inferred from homology;
KW Antibiotic resistance; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..652
FT /note="Tetracycline resistance protein TetP"
FT /id="PRO_0000091508"
FT DOMAIN 2..252
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 11..18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 75..79
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 129..132
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 652 AA; 72723 MW; EFE5E1113D562113 CRC64;
MKKIINIGIV AHVDAGKTTI TENLLYYSGA IKSVGRVDLG NTQTDSMELE RKRGITIKSS
TISFNWNNVK VNIIDTPGHV DFISEVERSL NSLDGAILVI SGVEGIQSQT RILFDTLKEL
NIPTIIFVNK LDRIGANFNK VFEEIKKNMS NKVVRLQEVY DVGSKAVYIK KLFDTCIIND
DAINVLSDLD EAFLERYIGG IEPDKEEIQE KLSLYAREGS LYPVFCGAAA IGLGIEDLLD
GICSYFPFAS NDCESDLSGV VFKIERTSKN EKKVYVRLFG GKISVRDKIQ VPNKEIAEKV
KKINRLENGG VVEAQRIEAG DIGILYGLTS FQVGDVIGIS NDKIKNISIA KPALKTTISA
IDKEKNPELF KALTLLAEED PLLAFAMNDI DKEIYVNLFG EVQMEILSSM LDDLYGIKVE
FSNIETIYKE TPKGFGASIM HMQEDLNPFW ATVGLEIEPA GRGEGLRYIS NVSVGSLPKS
FQNAIEEAVI KTSKQGLFGW EVTDVKVTLS CGEFFSPAST PADFRNVTPM VFMEALYKAQ
TVLLEPLHEF ELKIPQNALS KAVWDLETMR ATFDNPIVIG DEFSIKGLIP VENSKEYKMK
IASYTEGRGM FVTKFYGYKE ASAEFSKARK KTTYDPLNKK EYLLHKLNAI RD
//
