ID R9MTW6_9FIRM Unreviewed; 913 AA.
AC R9MTW6;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Small GTP-binding protein domain protein {ECO:0000313|EMBL:EOS71217.1};
GN ORFNames=C818_01225 {ECO:0000313|EMBL:EOS71217.1};
OS Lachnospiraceae bacterium MD308.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1235799 {ECO:0000313|EMBL:EOS71217.1, ECO:0000313|Proteomes:UP000014117};
RN [1] {ECO:0000313|EMBL:EOS71217.1, ECO:0000313|Proteomes:UP000014117}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3-2 {ECO:0000313|EMBL:EOS71217.1,
RC ECO:0000313|Proteomes:UP000014117};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium 3-2.";
RL Submitted (APR-2013) 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:EOS71217.1}.
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DR EMBL; ASTE01000011; EOS71217.1; -; Genomic_DNA.
DR AlphaFoldDB; R9MTW6; -.
DR STRING; 1235799.C818_01225; -.
DR PATRIC; fig|1235799.3.peg.1308; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_5_0_9; -.
DR OrthoDB; 9801472at2; -.
DR Proteomes; UP000014117; 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: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 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 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:UP000014117}.
FT DOMAIN 6..235
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 659..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 913 AA; 102961 MW; B0BDF01F9BE1C6D1 CRC64;
MFRNYDEKIV IGILAHVDAG KTTLSESILY LTGRIRKQGR VDHGDAFLDN YELEKNRGIT
IFSKQAVFPL GELTVTLLDT PGHVDFSAEM ERTLKVLDAA VLVINGADGV QGHTRTLWRL
LSIYRIPVFL FINKMDQEGT DKLALLKELA RSLDEGCVSF DVPEDSFYEE IALCSEDAME
QYLETGRLEE ETIAEMIAGR KVFPCYFGAA LKNEGVQKLL EGIEKYAGAC IGRQSSRGEE
DKEKREGFGA RVFKISRDSR GSRLTHIKIT AGKLCVKDIL VDEEKVNQIR IYSGEKYEMV
QEAQAGMVCA VTGLNGTYAG QGLGTEEDSE SPFLEPVLNY QVLLPDGFDV HKMLVCLRQL
EEEDPMLKVV WNEELGEIHV RLMGEVQTEI LKSLIQERFG VSVEFGTGNI VYKETIQKTA
EGVGHYEPLR HYAEVHLILE PAEPGSGLSF HTACSEDELD KNWQRLILTH LTEKPHRGVL
TGSVVTDMKI TLAAGRAHLK HTEGGDFRQS TYRAVRQGLM QAESILLEPY YTYRLEIPAE
MTGRAMTDIQ RMNGETDTPK TAGEMTVLSG KAPVAAMRDY QREVLGYTRG RGRLTLAFRD
YEPCHNQEEV IEEIGYDPEK DMDNPSGSVF CAHGAGFYVP WHEVPAHMHI ESQLKKWMPE
EADKPESETL GRRGKGAGRL PAGKEAAQMY SQSRKEEKEL EDIFIRTYGK YETKTAPAAR
TVASSAEKRQ KKKEPLKEYL LVDGYNVIFA WEDLKELAKD NIEGARGKLM DILCNYQGFK
KCTVILVFDA YKVDGYILEI QKYHNIHVVY TKEAETADQY IEKVVHEIGR KYHVTVVTSD
GVEQVVTLGQ GGTLLSAREF LEEVKLVRKQ MEEEYGSGAR GTKNYLFDTM DEELLKEMEE
VRLGKKELGG NKK
//
