ID A0A2K4ZJY8_9FIRM Unreviewed; 629 AA.
AC A0A2K4ZJY8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Tetracycline resistance protein TetO {ECO:0000313|EMBL:SOY30798.1};
GN Name=tetO_1 {ECO:0000313|EMBL:SOY30798.1};
GN ORFNames=AMURIS_03529 {ECO:0000313|EMBL:SOY30798.1};
OS Acetatifactor muris.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Acetatifactor.
OX NCBI_TaxID=879566 {ECO:0000313|EMBL:SOY30798.1, ECO:0000313|Proteomes:UP000236311};
RN [1] {ECO:0000313|EMBL:SOY30798.1, ECO:0000313|Proteomes:UP000236311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GP69 {ECO:0000313|EMBL:SOY30798.1};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; OFSM01000019; SOY30798.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K4ZJY8; -.
DR OrthoDB; 9801472at2; -.
DR Proteomes; UP000236311; 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:0006412; P:translation; IEA:UniProtKB-KW.
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; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
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 PRINTS; PR00315; ELONGATNFCT.
DR PRINTS; PR01037; TCRTETOQM.
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 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:UP000236311}.
FT DOMAIN 1..248
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 629 AA; 71469 MW; 7001C514EF3CACDD CRC64;
MNVINLGILA HVDAGKTTLT EGMLFQAGCI RKMGNVDDGT TVTDSMDLEK KRGMTIKSSV
ISFEWNHMKI NLIDTPGHFD FLSQVESVLH VLDVVVLVIA AREGVQPQTR LFFRKLSELN
IPTVIFINKL DRMGVNYEDL IKTIRTKLTD EILECQRYQG VGGKQVEIED IPLEDEELQM
KLLLSSETLL KKYDESQEIT TKEYETELIR LVRGGKLYPV LGGVALKNQG ITSLMDMLTK
IMADVKPQTD KLSAYVFKVD FDQKGQKRIF FRVFSGTVTV RQNVYIRNEE SQKMLVRNLA
YFENGKIISA RSVACGDVGI IYDEELLKVG TVIGGNHGDD SKVKLKEPLF HANIVAKDNN
ERYRLLNALN TLWQEDPQLK FEVSSMTEDI IISLYGPLQM EILGEILKNR FGLNISFGPL
TNIYKEHPTK EGYCSMRIGD WKNPYYAGVV FQVEPLPLGS GFQYENLVSY GYLEKPFQNA
VMDGIRIALN EGTQGHEVID VKITFLEADY DSVMGTPADF RRLVPVALKK AFDDSNVEML
EPWQSFIISV PVDYDKTVLN DICKMKARIT EYQYGETETC FIGKALLQDM MNYESRLNIL
THGSATVLQD FFKYLPMNES VEALMEKYK
//
