ID E4KZU8_9FIRM Unreviewed; 346 AA.
AC E4KZU8;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Elongation factor G C-terminal domain protein {ECO:0000313|EMBL:EFR32558.1};
GN ORFNames=HMPREF9286_0182 {ECO:0000313|EMBL:EFR32558.1};
OS Peptoniphilus harei ACS-146-V-Sch2b.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=908338 {ECO:0000313|EMBL:EFR32558.1, ECO:0000313|Proteomes:UP000003705};
RN [1] {ECO:0000313|EMBL:EFR32558.1, ECO:0000313|Proteomes:UP000003705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-146-V-Sch2b {ECO:0000313|EMBL:EFR32558.1,
RC ECO:0000313|Proteomes:UP000003705};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (OCT-2010) 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:EFR32558.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AENP01000025; EFR32558.1; -; Genomic_DNA.
DR AlphaFoldDB; E4KZU8; -.
DR eggNOG; COG0480; Bacteria.
DR Proteomes; UP000003705; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR CDD; cd03711; Tet_C; 1.
DR CDD; cd16258; Tet_III; 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 InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR035650; Tet_C.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
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 PRINTS; PR01037; TCRTETOQM.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 4: Predicted;
KW Elongation factor {ECO:0000313|EMBL:EFR32558.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:EFR32558.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003705}.
FT DOMAIN 124..239
FT /note="Translation elongation factor EFG/EF2"
FT /evidence="ECO:0000259|SMART:SM00889"
SQ SEQUENCE 346 AA; 39467 MW; 5B6B4F5C009BC4EA CRC64;
MYTSINGELC KIDRAYSGEI VILQNEFLKL NSVLGDTKLL PQRKKIENPH PLLQTTVEPS
KPEQREMLLD ALLEISDSDP LLRYYVDSTT HEIILSFLGK VQMEVISALL QEKYHVEIEL
KEPTVIYMER PLKNAEYTIH IEVPPNPFWA SIGLSVSPLP LGSGMQYESS VSLGYLNQSF
QNAVMEGIRY GCEQGLYGWN VTDCKICFKY GLYYSPVSTP ADFRMLAPIV LEQVLKKAGT
ELLEPYLSFK IYAPQEYLSR AYNDAPKYCA NIVDTQLKNN EVILSGEIPA RCIQEYRSDL
TFFTNGRSVC LTELKGYHVT TGEPVCQPRR PNSRIDKVRY MFNKIT
//
