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Database: UniProt
Entry: U5MSC7_CLOSA
LinkDB: U5MSC7_CLOSA
Original site: U5MSC7_CLOSA 
ID   U5MSC7_CLOSA            Unreviewed;       724 AA.
AC   U5MSC7;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Tetracycline resistance protein TetP {ECO:0000313|EMBL:AGX42551.1};
GN   Name=tetP {ECO:0000313|EMBL:AGX42551.1};
GN   ORFNames=CLSA_c15510 {ECO:0000313|EMBL:AGX42551.1};
OS   Clostridium saccharobutylicum DSM 13864.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1345695 {ECO:0000313|EMBL:AGX42551.1, ECO:0000313|Proteomes:UP000017118};
RN   [1] {ECO:0000313|EMBL:AGX42551.1, ECO:0000313|Proteomes:UP000017118}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13864 {ECO:0000313|EMBL:AGX42551.1};
RX   PubMed=24285650;
RA   Poehlein A., Hartwich K., Krabben P., Ehrenreich A., Liebl W., Durre P.,
RA   Gottschalk G., Daniel R.;
RT   "Complete Genome Sequence of the Solvent Producer Clostridium
RT   saccharobutylicum NCP262 (DSM 13864).";
RL   Genome Announc. 1:e00997-13(2013).
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; CP006721; AGX42551.1; -; Genomic_DNA.
DR   RefSeq; WP_022744890.1; NZ_AYXL01000320.1.
DR   AlphaFoldDB; U5MSC7; -.
DR   GeneID; 55474050; -.
DR   KEGG; csb:CLSA_c15510; -.
DR   PATRIC; fig|1345695.10.peg.3660; -.
DR   eggNOG; COG0480; Bacteria.
DR   HOGENOM; CLU_002794_5_1_9; -.
DR   OrthoDB; 9801472at2; -.
DR   Proteomes; UP000017118; Chromosome.
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; 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; IPR035647; EFG_III/V.
DR   InterPro; IPR000640; EFG_V-like.
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; 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; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000017118}.
FT   DOMAIN          1..259
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   724 AA;  83002 MW;  F4F4FF1AE8E35735 CRC64;
     MKKTIGVLAH VDAGKTTFSE QVLYHTNSIR SRGRVDHKDA FLDSHSIERK RGITVFSDQA
     VFKFSDSTYY LIDTPGHVDF STEMERSIGI MDYAIIIISA VEGVQGHTKT VWRLLEKYKI
     PTFFFINKLD RVGADKDKVI EEIKKNLTKD ICYIDKSSIK FKADKEFNYE SKVNNSNTQN
     VQNNYLDLND EIIEFISEYD EVLLEKYLDG EYDEKLWKNV FRNLIKENKV FPCFAGSALQ
     DEGILEFIYG LDELTFTNYE DLNIADCNDN SSLMPMFRDN ILNTTNKFAG YVYKVRHEAT
     GNRITFIKCL KGELKVRDEI IHGGEIKANN YSNEMEKSDN SKLQLSFEYG NEIKEKVSSI
     RIYNGNKFKA VDNVKAGDVF GVTGLTNVLP GEGIGELRLK TNYEMVPTLM SKVIFDAFYN
     IKEVLGYFKL LEAEDPALNV IWSEAIQEMH VHIMGKIQLE VLKEIVEERF NLSVEFGPCE
     ILYKESILET AIGSGHFEPL RHYAEVHLKI EPLPRNSGII FDNKCHSDHL TIGNQNLIKT
     HIFEREHHGI LTGSPLTDIK ITLLTGRAHL KHTSGGDFRE ATFRALRQGL EKVENILLEP
     YYKFTIEVEQ DFIGRVLSDI QKMDGTFDAP EIAKDKMIVN GRGPVARFMD YPMEVIAFTK
     GKGHINLIYD GYDNCHNSEE VIQKRDYNKN ADIEYTSSSI FCSHGQGYIV EWDEADKSMH
     CELE
//
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