ID E8JT07_STRCR Unreviewed; 644 AA.
AC E8JT07;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Putative translation elongation factor G {ECO:0000313|EMBL:EFX53501.1};
GN Name=tetP {ECO:0000313|EMBL:EFX53501.1};
GN ORFNames=HMPREF9422_0337 {ECO:0000313|EMBL:EFX53501.1};
OS Streptococcus cristatus ATCC 51100.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=889201 {ECO:0000313|EMBL:EFX53501.1, ECO:0000313|Proteomes:UP000002829};
RN [1] {ECO:0000313|EMBL:EFX53501.1, ECO:0000313|Proteomes:UP000002829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51100 {ECO:0000313|EMBL:EFX53501.1,
RC ECO:0000313|Proteomes:UP000002829};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (DEC-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:EFX53501.1}.
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; AEVC01000006; EFX53501.1; -; Genomic_DNA.
DR AlphaFoldDB; E8JT07; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_2_9; -.
DR Proteomes; UP000002829; 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 CDD; cd03690; Tet_II; 1.
DR CDD; cd16258; Tet_III; 1.
DR CDD; cd01684; Tet_like_IV; 1.
DR CDD; cd04168; TetM_like; 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; 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; 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; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Elongation factor {ECO:0000313|EMBL:EFX53501.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 6..247
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 644 AA; 73120 MW; 41719067F57BBCF1 CRC64;
MEENHMKIIN IGVLAHVDAG KTTLTESLLY NSGAITELGS VDKGTTRTDN TLLERQRGIT
IQTGITSFQW ENTKVNIIDT PGHMDFLAEV YRSLSVLDGA ILLISAKDGV QAQTRILFHA
LRKMGIPTIF FINKIDQNGI DLSTVYQDIK EKLSAEIVIK QKVELYPNMC VTNFTESEQW
DTVIEGNDDL LEKYMSGKSL EALELEQEES IRFQNCSLFP VYHGSAKSNI GIDNLIEVIT
NKFYSSTHRG PSELCGNVFK IEYSEKRQRL AYIRLYSGVL HLRDSVRISE KEKIKITEMY
TSINGELCKI DKAYSGEIVI LQNEFLKLNS VLGDTKLLPQ RKKIENPHPL LQTTVEPSKP
EQREMLLDAL LEISDSDPLL RYYVDSTTHE IILSFLGKVQ MEVISALLQE KYHVEIELKE
PTVIYMERPL KNAEYTIHIE VPPNPFWASI GLSVAQLPLG SGVQYESSVS LGYLNQSFQN
AVMEGIRYGC EQGLYGWNVT DCKICFKYGL YYSPVSTPAD FRMLAPIVLE QVLKKAGTEL
LEPYLSFKIY APQEYLSRAY NDAPKYCANI VDTQLKNNEV ILSGEIPARC IQEYRSDLTF
FTNGRSVCLT ELKGYHVTTG EPVCQPRRPN SRIDKVRYMF NKIT
//
