ID   RF3_STRMU               Reviewed;         514 AA.
AC   Q8DV91;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Peptide chain release factor 3 {ECO:0000255|HAMAP-Rule:MF_00072};
DE            Short=RF-3 {ECO:0000255|HAMAP-Rule:MF_00072};
GN   Name=prfC {ECO:0000255|HAMAP-Rule:MF_00072}; OrderedLocusNames=SMU_608;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC   -!- FUNCTION: Increases the formation of ribosomal termination complexes
CC       and stimulates activities of RF-1 and RF-2. It binds guanine
CC       nucleotides and has strong preference for UGA stop codons. It may
CC       interact directly with the ribosome. The stimulation of RF-1 and RF-2
CC       is significantly reduced by GTP and GDP, but not by GMP.
CC       {ECO:0000255|HAMAP-Rule:MF_00072}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00072}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. PrfC subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00072}.
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DR   EMBL; AE014133; AAN58346.1; -; Genomic_DNA.
DR   RefSeq; NP_721040.1; NC_004350.2.
DR   RefSeq; WP_002263242.1; NC_004350.2.
DR   AlphaFoldDB; Q8DV91; -.
DR   SMR; Q8DV91; -.
DR   STRING; 210007.SMU_608; -.
DR   PRIDE; Q8DV91; -.
DR   EnsemblBacteria; AAN58346; AAN58346; SMU_608.
DR   GeneID; 66817925; -.
DR   KEGG; smu:SMU_608; -.
DR   PATRIC; fig|210007.7.peg.540; -.
DR   eggNOG; COG4108; Bacteria.
DR   HOGENOM; CLU_002794_2_1_9; -.
DR   OMA; GFVFKIH; -.
DR   PhylomeDB; Q8DV91; -.
DR   Proteomes; UP000002512; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule.
DR   GO; GO:0006449; P:regulation of translational termination; IEA:UniProtKB-UniRule.
DR   CDD; cd04169; RF3; 1.
DR   Gene3D; 3.30.70.3280; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00072; Rel_fac_3; 1.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004548; PrfC.
DR   InterPro; IPR032090; RF3_C.
DR   InterPro; IPR038467; RF3_dom_3_sf.
DR   InterPro; IPR041732; RF3_GTP-bd.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   PANTHER; PTHR43556; PTHR43556; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF16658; RF3_C; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54980; SSF54980; 1.
DR   TIGRFAMs; TIGR00503; prfC; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..514
FT                   /note="Peptide chain release factor 3"
FT                   /id="PRO_0000210971"
FT   DOMAIN          8..268
FT                   /note="tr-type G"
FT   BINDING         17..24
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT   BINDING         85..89
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT   BINDING         139..142
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
SQ   SEQUENCE   514 AA;  58564 MW;  77CCE23BB5C93946 CRC64;
     MNLQEEIKKR RTFAIISHPD AGKTTITEQL LYFGGEIREA GTVKGKKTGN FAKSDWMDIE
     KQRGISVTSS VMQFDYAGKR VNILDTPGHE DFSEDTYRTL MAVDAAVMVV DSAKGIEAQT
     KKLFEVVKHR GIPIFTFINK LDRDGREPLD LLEELEEVLG IASYPMNWPI GMGRSFEGLY
     DLYNQRLELY KGDERFASIE DGDKLFANNP FYEQAKEDIE LLTEAGNEFS EEAILKGELT
     PVFFGSALTN FGVQTFLDSF LAFAPEPHGH KTTDDKVIDP LDKDFSGFVF KIQANMDPRH
     RDRIAFVRIV SGEFERGMSV NLARTGKSVK LSNVTQFMAE SRENVENAVA GDIIGVYDTG
     TYQVGDTLTV GKNKFEFEPL PTFTPELFMK VSAKNVMKQK SFHKGIEQLV QEGAIQLYTN
     YQTGEYMLGA VGQLQFEVFK HRMENEYNAE VIMTPMGKKT VRWIKEEDLD ERMSSSRNIL
     AKDRFNKPVF LFENDFSLHW FADKYPDIVL EEKM