ID A0A0R2I273_9LACO Unreviewed; 643 AA.
AC A0A0R2I273;
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:KRN59280.1};
GN ORFNames=IV45_GL001428 {ECO:0000313|EMBL:KRN59280.1};
OS Limosilactobacillus secaliphilus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=396268 {ECO:0000313|EMBL:KRN59280.1, ECO:0000313|Proteomes:UP000050934};
RN [1] {ECO:0000313|EMBL:KRN59280.1, ECO:0000313|Proteomes:UP000050934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17896 {ECO:0000313|EMBL:KRN59280.1,
RC ECO:0000313|Proteomes:UP000050934};
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:KRN59280.1}.
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DR EMBL; JQBW01000005; KRN59280.1; -; Genomic_DNA.
DR RefSeq; WP_057740040.1; NZ_JQBW01000005.1.
DR AlphaFoldDB; A0A0R2I273; -.
DR STRING; 396268.IV45_GL001428; -.
DR PATRIC; fig|396268.3.peg.1449; -.
DR OrthoDB; 9801591at2; -.
DR Proteomes; UP000050934; 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; 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:KRN59280.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:KRN59280.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050934}.
FT DOMAIN 1..230
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 643 AA; 70438 MW; 844CC4CDC34A5D4B CRC64;
MKKITMGIVA PVDAGKTTLS EEMLYQTGTI RHAGRVDHGD TFLDPAAIEK QRGITVFAHQ
AELTMDDVSM TLLDTPGHVD FAATTEQVLP VLDYAILIVA GSDGVTGYTR LLWRLLTRYQ
VPTFIFVNKV DAPGFDRQRV MKELQALDDG CLPFGQQLSE QTLEDVASQD ETALEEYLKQ
GSLTDAQVQQ LIAQRKVFPV YFGSALKQTG VSELLDGLAK WTLGRQWPSE FGARVFKISH
DKDGSQLTWL RVTGGALQAK QTLVDDEKAD ALRVYNGEKY DVVQQVPAGG VCAVVGPEKL
VAGQGLGEDS GSQTALLKPV LAYTVVIDHD QHDCLQKLQE LSLDDPQLKV VWNSELKAIT
VQVMGPMQLE VLAQLLKDRY QIDVHFEKGT VLYQETVTEA IEGVGHFEPL RHYSECHLLI
EPGKQGSGLQ FAINCSVDVL GHNYQQQIMT ALKSKLQRGV LIGAPLTDAK ITLVGGRASV
VHSVGGDFRE AANRALRQGL MELKQKAACQ LLEPWYRFTL LVPNDQVGRA LNDIQRASGD
FDAPAPLANN QTQITGHAPV SEIRDYAATV RGYTHGEGQL ACVPAGNRPC HNAEAVIADA
GYDPVADLAN TPDSVFCAHG AGYPVHWDQV PNKMHCDYYT DFH
//
