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Database: UniProt
Entry: A0A0R2LJD7_9LACO
LinkDB: A0A0R2LJD7_9LACO
Original site: A0A0R2LJD7_9LACO 
ID   A0A0R2LJD7_9LACO        Unreviewed;       654 AA.
AC   A0A0R2LJD7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Translation elongation factor (GTPase) {ECO:0000313|EMBL:KRO01654.1};
GN   ORFNames=IV66_GL002170 {ECO:0000313|EMBL:KRO01654.1};
OS   Ligilactobacillus pobuzihii.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=449659 {ECO:0000313|EMBL:KRO01654.1, ECO:0000313|Proteomes:UP000051886};
RN   [1] {ECO:0000313|EMBL:KRO01654.1, ECO:0000313|Proteomes:UP000051886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 103219 {ECO:0000313|EMBL:KRO01654.1,
RC   ECO:0000313|Proteomes:UP000051886};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:KRO01654.1}.
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DR   EMBL; JQCN01000007; KRO01654.1; -; Genomic_DNA.
DR   RefSeq; WP_017867189.1; NZ_JQCN01000007.1.
DR   AlphaFoldDB; A0A0R2LJD7; -.
DR   STRING; 449659.IV66_GL002170; -.
DR   PATRIC; fig|449659.4.peg.2231; -.
DR   OrthoDB; 9801591at2; -.
DR   Proteomes; UP000051886; 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; 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; 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   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; 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; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   Elongation factor {ECO:0000313|EMBL:KRO01654.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:KRO01654.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051886}.
FT   DOMAIN          1..237
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   654 AA;  72668 MW;  6A93A525059C603F CRC64;
     MKQIVTGIVA HVDAGKTTLS EALLYQTGSL RQLGRVDDQN TFLDPEKLEK QRGITIFSHQ
     ARLISNDLEL TLLDTPGHVD FAAQTEQVLS VLDYAVLVVS ASSGIQGYTL ILWRLLARYH
     VPVFIFVNKM DTTERNRQQI IEQLQKEFSP GCLDFTKAFA QKGDFNQLND EFCESVALCD
     ADVLDGYLEN SELSAETIQQ MIIERQVFPC YFGSALKMTG TAELLLGMEY WTKQPPVVNQ
     PFGALVFKVS HSKNDERLTW VRLTSGSLHP KEILLGEQKV NQLRIYNGSK YEVLPEVTCG
     QVCAIPGLKE TYPSQGLGSQ KDAVQPQLTP VLTYVVDKKG QDVQVCLKAL RQLQDEDPQL
     HVTWSEELKE IQVQLMGEIQ IEVLTNILME RFGLDLGFDQ GSILYKESIK SPVEGVGHFE
     PLRHYAEVHL RLEPAPAGSG LTFASECSLE VLASNWQHQV LSNLQAKQHL GVLLGVPLTD
     MKITLVSGKA SNVHTVGGDF REATWRAVRQ GLMELRQQDQ CVLLEPWYRF NLQVGSEQVG
     RAMTDIERMS GQFKIPGNSA ENSGLVTLTG QAPVSEMQDY AAKVRAYTHG KGQLECVFAG
     YFPCHNTTEV VAQQGYDPGS DLNNTPGSIF CAHGAGYPVA WNKVPEMAHV GYSN
//
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