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   03-AUG-2022, entry version 104.
DE   RecName: Full=Tetracycline resistance protein TetP;
DE   AltName: Full=TetB(P);
GN   Name=tetP; Synonyms=tetB(P);
OS   Clostridium perfringens.
OC   Bacteria; Firmicutes; 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   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 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_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_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   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   SMART; SM00838; EFG_C; 1.
DR   SMART; SM00889; EFG_IV; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF54980; SSF54980; 2.
DR   TIGRFAMs; TIGR00231; small_GTP; 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