RF3_STAAC
ID RF3_STAAC Reviewed; 520 AA.
AC O86490; Q5HH66;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Peptide chain release factor 3;
DE Short=RF-3;
DE Short=RF3;
GN Name=prfC; OrderedLocusNames=SACOL1025;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9650993; DOI=10.1089/mdr.1998.4.85;
RA Ludovice A.M., Wu S.-W., de Lencastre H.;
RT "Molecular cloning and DNA sequencing of the Staphylococcus aureus UDP-N-
RT acetylmuramyl tripeptide synthetase (murE) gene, essential for the optimal
RT expression of methicillin resistance.";
RL Microb. Drug Resist. 4:85-90(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. PrfC subfamily.
CC {ECO:0000305}.
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DR EMBL; Y14370; CAA74739.1; -; Genomic_DNA.
DR EMBL; CP000046; AAW36491.1; -; Genomic_DNA.
DR RefSeq; WP_001049959.1; NC_002951.2.
DR AlphaFoldDB; O86490; -.
DR SMR; O86490; -.
DR EnsemblBacteria; AAW36491; AAW36491; SACOL1025.
DR KEGG; sac:SACOL1025; -.
DR HOGENOM; CLU_002794_2_1_9; -.
DR OMA; GFVFKIH; -.
DR Proteomes; UP000000530; 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.
FT CHAIN 1..520
FT /note="Peptide chain release factor 3"
FT /id="PRO_0000210962"
FT DOMAIN 8..277
FT /note="tr-type G"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 85..89
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 139..142
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 48..55
FT /note="TGKFATSD -> LVNLRQVT (in Ref. 1; CAA74739)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="K -> E (in Ref. 1; CAA74739)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="I -> V (in Ref. 1; CAA74739)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="Q -> P (in Ref. 1; CAA74739)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="D -> N (in Ref. 1; CAA74739)"
FT /evidence="ECO:0000305"
FT CONFLICT 322..349
FT /note="GMDVTLQRTNKKQKITRSTSFMADDKET -> VWMLLCNVLIKSKRSHVQRH
FT LWQTIKKL (in Ref. 1; CAA74739)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="W -> WD (in Ref. 1; CAA74739)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 59602 MW; B1EA5947ACA4F541 CRC64;
MNLKQEVESR KTFAIISHPD AGKTTLTEKL LYFSGAIREA GTVKGKKTGK FATSDWMKVE
QERGISVTSS VMQFDYDDYK INILDTPGHE DFSEDTYRTL MAVDSAVMVI DCAKGIEPQT
LKLFKVCKMR GIPIFTFINK LDRVGKEPFE LLDEIEETLN IETYPMNWPI GMGQSFFGII
DRKSKTIEPF RDEENILHLN DDFELEEDHA ITNDSDFEQA IEELMLVEEA GEAFDNDALL
SGDLTPVFFG SALANFGVQN FLNAYVDFAP MPNARQTKED VEVSPFDDSF SGFIFKIQAN
MDPKHRDRIA FMRVVSGAFE RGMDVTLQRT NKKQKITRST SFMADDKETV NHAVAGDIIG
LYDTGNYQIG DTLVGGKQTY SFQDLPQFTP EIFMKVSAKN VMKQKHFHKG IEQLVQEGAI
QYYKTLHTNQ IILGAVGQLQ FEVFEHRMKN EYNVDVVMEP VGRKIARWIE NEDQITDKMN
TSRSILVKDR YDDLVFLFEN EFATRWFEEK FPEIKLYSLL
