TETO_CAMJU
ID TETO_CAMJU Reviewed; 639 AA.
AC P10952;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Tetracycline resistance protein TetO;
DE Short=Tet(O);
GN Name=tetO; Synonyms=tet(O);
OS Campylobacter jejuni.
OG Plasmid pUA466.
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=197;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2836268; DOI=10.1016/0378-1119(88)90576-8;
RA Manavathu E.K., Hiratsuka K., Taylor D.E.;
RT "Nucleotide sequence analysis and expression of a tetracycline-resistance
RT gene from Campylobacter jejuni.";
RL Gene 62:17-26(1988).
RN [2]
RP SEQUENCE REVISION TO 591 AND 636-639.
RA Manavathu E.K., Hiratsuka K., Taylor D.E.;
RL Submitted (JUN-2003) 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 -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. TetM/TetO
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; M18896; AAA23033.2; -; Genomic_DNA.
DR PIR; A29809; A29809.
DR RefSeq; WP_002779752.1; NZ_SYTG01000001.1.
DR PDB; 4V6V; EM; 9.80 A; A1=1-639.
DR PDBsum; 4V6V; -.
DR AlphaFoldDB; P10952; -.
DR SMR; P10952; -.
DR KEGG; ag:AAA23033; -.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR CDD; cd03711; Tet_C; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_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 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 SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; GTP-binding; Nucleotide-binding;
KW Plasmid; Protein biosynthesis.
FT CHAIN 1..639
FT /note="Tetracycline resistance protein TetO"
FT /id="PRO_0000091505"
FT DOMAIN 1..244
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 74..78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 128..131
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 639 AA; 72563 MW; 2B5A48484E2CFA01 CRC64;
MKIINLGILA HVDAGKTTLT ESLLYTSGAI AELGSVDEGT TRTDTMNLER QRGITIQTAV
TSFQWEDVKV NIIDTPGHMD FLAEVYRSLS VLDGAVLLVS AKDGIQAQTR ILFHALQIMK
IPTIFFINKI DQEGIDLPMV YREMKAKLSS EIIVKQKVGQ HPHINVTDND DMEQWDAVIM
GNDELLEKYM SGKPFKMSEL EQEENRRFQN GTLFPVYHGS AKNNLGTRQL IEVIASKFYS
STPEGQSELC GQVFKIEYSE KRRRFVYVRI YSGTLHLRDV IRISEKEKIK ITEMYVPTNG
ELYSSDTACS GDIVILPNDV LQLNSILGNE ILLPQRKFIE NPLPMIQTTI AVKKSEQREI
LLGALTEISD CDPLLKYYVD TTTHEIILSF LGNVQMEVIC AILEEKYHVE AEIKEPTVIY
MERPLRKAEY TIHIEVPPNP FWASVGLSIE PLPIGSGVQY ESRVSLGYLN QSFQNAVMEG
VLYGCEQGLY GWKVTDCKIC FEYGLYYSPV STPADFRLLS PIVLEQALKK AGTELLEPYL
HFEIYAPQEY LSRAYHDAPR YCADIVSTQI KNDEVILKGE IPARCIQEYR NDLTYFTNGQ
GVCLTELKGY QPAIGKFICQ PRRPNSRIDK VRHMFHKLA