ID U2BPX7_CLOSY Unreviewed; 898 AA.
AC U2BPX7;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Putative translation elongation factor G {ECO:0000313|EMBL:ERI74275.1};
GN ORFNames=CLOSYM_04193 {ECO:0000313|EMBL:ERI74275.1};
OS [Clostridium] symbiosum ATCC 14940.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=411472 {ECO:0000313|EMBL:ERI74275.1, ECO:0000313|Proteomes:UP000016491};
RN [1] {ECO:0000313|EMBL:ERI74275.1, ECO:0000313|Proteomes:UP000016491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14940 {ECO:0000313|EMBL:ERI74275.1,
RC ECO:0000313|Proteomes:UP000016491};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (JUL-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:ERI74275.1}.
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DR EMBL; AWSU01000339; ERI74275.1; -; Genomic_DNA.
DR RefSeq; WP_021641362.1; NZ_KE992855.1.
DR AlphaFoldDB; U2BPX7; -.
DR PATRIC; fig|411472.5.peg.3922; -.
DR HOGENOM; CLU_002794_5_0_9; -.
DR Proteomes; UP000016491; 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:ERI74275.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 1..227
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 638..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 898 AA; 100536 MW; 951D90A21C0FC42C CRC64;
MKKLAVGILA HVDAGKTTLS EAMLYTGGAV RKLGRVDKGD AFLDTYELEK KRGITIFSKQ
AILEWNGMQV TLLDTPGHVD FSAEMERTLQ VLDYAVLVIS GTDGVQGHTQ TLWRLLARYK
IPAFLFVNKM DLAGERKEAI LEELTRKLDG NIVDFGEQGT EGFYENLAMC GEAALDQFLE
NGMIHRDDVT KMILTRQVFP CFFGSALKLD GIEAFMQGME DYMSMPDYPS EFGAKVFKIA
RDNQGNRLTY MKITGGSLKV RELIGEEKVN QIRIYSGEKF EAVQEAKAGT VCAVTGPSGT
VPGKGIGIEE AGAMPVLEPV LTYRIQLPEE ADAAVMLPKL AQLEEEEPQL HITWQEEAKE
IHAQIMGEIQ MEILKGLVRE RFGINIEFGG RSIVYKETIQ NTVEGVGHFE PLRHYAEVHL
LMEPAEAGSG LSFSTECSED VLDRNWQRLI LTHLEEREHK GVLTGSAITD MKITLMSGRA
HLKHTEGGDF RQAVYRAVRQ GLMQADSVLL EPVYGFRLEV PERMLGRAMT DVERMHGQFE
PPVMEGEYAV LSGSAPVACM DGYQQEMTAY TGGLGRLACT LKGYAPCHNA DEVIEASGYD
ADSDTENPSG SVFCAHGAGF VVSWDEVPDY MHLESCLPPE ISEGNDGEDG SGTAGRNGRK
KRRKDEGHEE IWLGTDEIDE ILARTYHANK RDKTGAQKRR WGSKSKTPSG TYTAGRLSGT
GATAARLAKK EEKREQYLLI DGYNIIFAWE ELRELAERNI DSARGKLLDI LCNYQGAKKC
QVIAVFDAYR VQGHKTEFLD YHNIHVVYTK EAETADQYIE KFAHDNASKY DVTVATSDRL
EQIIIRGQGC RLISAREFWE ETERTNEEIR LEFEDKKPAE KQYMGEFIPE EIKRNMED
//