ID C6LJD8_9FIRM Unreviewed; 912 AA.
AC C6LJD8;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE SubName: Full=Putative translation elongation factor G {ECO:0000313|EMBL:EET59252.1};
GN ORFNames=BRYFOR_08774 {ECO:0000313|EMBL:EET59252.1};
OS Marvinbryantia formatexigens DSM 14469.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Marvinbryantia.
OX NCBI_TaxID=478749 {ECO:0000313|EMBL:EET59252.1, ECO:0000313|Proteomes:UP000005561};
RN [1] {ECO:0000313|EMBL:EET59252.1, ECO:0000313|Proteomes:UP000005561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14469 {ECO:0000313|EMBL:EET59252.1,
RC ECO:0000313|Proteomes:UP000005561};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JUL-2009) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EET59252.1}.
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DR EMBL; ACCL02000020; EET59252.1; -; Genomic_DNA.
DR AlphaFoldDB; C6LJD8; -.
DR STRING; 168384.SAMN05660368_03184; -.
DR eggNOG; COG0480; Bacteria.
DR Proteomes; UP000005561; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR CDD; cd10912; PIN_YacP-like; 1.
DR CDD; cd03711; Tet_C; 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 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 Elongation factor {ECO:0000313|EMBL:EET59252.1};
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:UP000005561}.
FT DOMAIN 20..245
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 655..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 912 AA; 101622 MW; 14162B697955ABBA CRC64;
MQKGAFSMGN SSENKSEKIK KHICVGILAH VDAGKTTLAE SMLYRQGSIR TMGRVDHGNA
FLDNYELERA RGITIFSKQA ILSLGDKEVT LLDTPGHVDF SAEMERTLQV LDYAILVISQ
ADGVQGHVLT LWKLLQRYQI PVFVFVNKMD QESAGREAVL AALQERLDGH CLDFGAPQGE
LKENLAMCDE ETLERYLETE TVTDEEIRRL IRERRVFPCC FGSALKNQGV EEFLAVLSGY
TSAPVYPEDF SARVYKISRD AQGNRLTHLK ITGGSLKVKT ALPAGKVDQI RIYSGANYQV
VQEAEAGSVC AVTGLADILP GEGLGAQTEG VQPALEPVLR YRVMLPEGCD VHGMLGKLRQ
LEEEDPLLRI SWEEDTGEIH AQVMGEVQME ILQSIIRERF GTEVSFGKGS IVYKETITKP
VEGVGHFEPL RHYAEVHLLL EPGERGSGLV FDTAVSEDEL DRNWQRLILT NLAEKKHVGV
LTGAQITDMK ITVIAGRAHL KHTEGGDFRE AAWRAVRQGL RSTESILLEP VYEFRLEVPQ
ENIGRAMADF TRMHGVFSQP EQEGDYSVLR GTVPASSVGD YQKEVTAYTK GRGRLFCSLK
GYEPCHNQEE IIAAAAYDPD ADTDNPSGSV FCAHGAGFYV PWDSVRDYMH VESHFSDGSR
EEPQEKQMAP VREKGASLGG WASDKELEEI FTRTYGAGKE ARSGWGRSRF SPARTAETGN
TGGPRRETPK EEYLLVDGYN IIFAWEELRE LARINIESAR GRLADILCNY QGFRKNTVIL
VFDAYRVEGG TGSVQKYHNI YVVYTREAET ADQYIEKTVH KISPQHHVTV ATSDALEQMI
IWGAGASRLS AAGLLEEIEA SCSEIRRDYL TGQKRTGEKL FDKLPEDLAA LMEDIRLGRR
SFAEQPEEKK NS
//
