RF3_LACH4
ID RF3_LACH4 Reviewed; 523 AA.
AC A8YU90;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=lhv_0681;
OS Lactobacillus helveticus (strain DPC 4571).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=405566;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DPC 4571;
RX PubMed=17993529; DOI=10.1128/jb.01295-07;
RA Callanan M., Kaleta P., O'Callaghan J., O'Sullivan O., Jordan K.,
RA McAuliffe O., Sangrador-Vegas A., Slattery L., Fitzgerald G.F.,
RA Beresford T., Ross R.P.;
RT "Genome sequence of Lactobacillus helveticus: an organism distinguished by
RT selective gene loss and IS element expansion.";
RL J. Bacteriol. 190:727-735(2008).
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; CP000517; ABX26828.1; -; Genomic_DNA.
DR RefSeq; WP_003627787.1; NC_010080.1.
DR AlphaFoldDB; A8YU90; -.
DR SMR; A8YU90; -.
DR STRING; 405566.lhv_0681; -.
DR EnsemblBacteria; ABX26828; ABX26828; lhv_0681.
DR GeneID; 66452687; -.
DR KEGG; lhe:lhv_0681; -.
DR eggNOG; COG4108; Bacteria.
DR HOGENOM; CLU_002794_2_1_9; -.
DR OMA; GFVFKIH; -.
DR Proteomes; UP000000790; 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; 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; 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..523
FT /note="Peptide chain release factor 3"
FT /id="PRO_1000071185"
FT DOMAIN 10..277
FT /note="tr-type G"
FT BINDING 19..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT BINDING 87..91
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
FT BINDING 141..144
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00072"
SQ SEQUENCE 523 AA; 59271 MW; 04F51126C440330A CRC64;
MDKELAEKVK KRRTFAIISH PDAGKTTITE QMLLFGGVIR KAGTVKARKT GNFATSDWME
IEKKRGISVT SSVMQFEYKG KRINILDTPG HQDFSEDTYR TLMAVDAAVM VIDSAKGIEP
QTKKLFKVVK KRGIPIFTFM NKLDRDGRPP LDLIAELEDL LGIEGVAMDW PIGSGQTLKG
LYDVANNRVE LYRKDGEDRF LPLNEDGTLP DSEPLSQDPQ FQDTLDEIEL VKEAGNKFDP
EKIALGDQTP VFFGSALTNF GVETFLNSFV DLAPAPESHT VNGDEELSPE DPEFSGFVFK
IQANMNPHHR DRIAFVRVGS GEFKRGLDVT LARTGKPIRL NNATEFMSSE RVQVSDAVAG
DIVGLYDTGN FQIGDSIYSG KRKIVYPPLP EFTPELFMRV TAKNVMKQKS FHKGMNQLVQ
EGAIQLYRNY QTDEYILGAV GQLQFEVFQF RMKNEYNSEV EMNSIGHRVA RWIDPEQLDP
RMSNSRNLLV KDRYGNPLFL FENEFAERFF HDKYPDVKLT EKL