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Database: UniProt
Entry: A0A078KNF2_9FIRM
LinkDB: A0A078KNF2_9FIRM
Original site: A0A078KNF2_9FIRM 
ID   A0A078KNF2_9FIRM        Unreviewed;       882 AA.
AC   A0A078KNF2;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Small GTP-binding domain protein {ECO:0000313|EMBL:CDZ24003.1};
GN   ORFNames=CCDG5_0878 {ECO:0000313|EMBL:CDZ24003.1};
OS   [Clostridium] cellulosi.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Oscillospiraceae incertae sedis.
OX   NCBI_TaxID=29343 {ECO:0000313|EMBL:CDZ24003.1, ECO:0000313|Proteomes:UP000032431};
RN   [1] {ECO:0000313|Proteomes:UP000032431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG5 {ECO:0000313|Proteomes:UP000032431};
RA   Wibberg D.;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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; LM995447; CDZ24003.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A078KNF2; -.
DR   STRING; 29343.CCDG5_0878; -.
DR   KEGG; ccel:CCDG5_0878; -.
DR   PATRIC; fig|29343.3.peg.936; -.
DR   HOGENOM; CLU_002794_5_0_9; -.
DR   OrthoDB; 9801472at2; -.
DR   Proteomes; UP000032431; 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; cd10912; PIN_YacP-like; 1.
DR   CDD; cd03711; Tet_C; 1.
DR   CDD; cd01684; Tet_like_IV; 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   InterPro; IPR010298; YacP-like.
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   Pfam; PF05991; NYN_YacP; 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   4: Predicted;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032431}.
FT   DOMAIN          1..227
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   COILED          830..857
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   882 AA;  100467 MW;  07D5B04377CBA3D8 CRC64;
     MKKLVIGILA HVDAGKTTLS EGMLYLSGKI RKLGRVDNKD SYLDTYELER QRGITIFSKQ
     AIFEVDDTQI TLLDTPGHVD FSAETERTLQ VLDYAVLVVS GADGVQGHTK TLWRLLEMYN
     IPVFIFINKM DQNGTDKDKL LREIKERMSN RCVEFEQINT TAFFEEIAMC DEELMDTYLE
     TGHIDTALIK KAIKKRKIYP CLFGSALKLE GVERLLHTVV EYTDEPSYPA EFGAKIFKIS
     RDSQGNRLTH LKVTGGKLKV KDILSGDSWK EKIDQIRIYS GEKFKTVNEI EAGGVCAVTG
     LSNSRPGEGL GIEKASNKPV LEPVLSYRII LPDGMDPRAM LPKLRQIEEE EPELHIVWDE
     RLQEIKVQVM GEVQTEILQS VIKNRFGVDV AFGEGKIVYK ETIANAVEGV GHFEPLRHYA
     EVHLLLEPGE PGSGLQFDTI CSEDLLSRNW QRLILTHLKE KEHKGVLTGS AITDMKITLV
     SGKASNKHTE GGDFREATYR AVRQGLKEAE SILLEPVYAF QLELPKKMVG RAMSDIENMH
     GTYKISQTDG ETVVLTGTAP VITMRNYQKE VAAYTGGLGR LFCSLKGYEP CHNAEEVIES
     IGYDSERDME NPTGSVFCAH GAGFLVDWYE VKNYMHLPSY FQDKTESEDE VVKHRTQKEE
     MNISPEEVDE ILKRTSYANQ RDKEKIKQKP KRESYSGPIN RVSIKKENKE EYLLVDGYNI
     IHAWPELKDL ADENMDGARM KLIETLSNYQ GYRKCQIIVV FDAYRVERHV EEAIDFNNIH
     IIYTREAQTA DQYIERFSHN NKKKYSITVA TSDALEQLIV RGAGCSLLSA NELKAEIEKT
     DRRIRQEYRQ INDENRNYLK DTLPSKTKRE MEEMINKGRG VK
//
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