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Database: UniProt
Entry: U2BPX7_CLOSY
LinkDB: U2BPX7_CLOSY
Original site: U2BPX7_CLOSY 
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
//
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