RF3_LACAC
ID RF3_LACAC Reviewed; 523 AA.
AC Q5FLA9;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=LBA0636;
OS Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=272621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA Hamrick A., Cano R., Klaenhammer T.R.;
RT "Complete genome sequence of the probiotic lactic acid bacterium
RT Lactobacillus acidophilus NCFM.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(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.
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; CP000033; AAV42515.1; -; Genomic_DNA.
DR RefSeq; WP_003546473.1; NC_006814.3.
DR RefSeq; YP_193546.1; NC_006814.3.
DR AlphaFoldDB; Q5FLA9; -.
DR SMR; Q5FLA9; -.
DR STRING; 272621.LBA0636; -.
DR EnsemblBacteria; AAV42515; AAV42515; LBA0636.
DR GeneID; 56942270; -.
DR KEGG; lac:LBA0636; -.
DR PATRIC; fig|272621.13.peg.608; -.
DR eggNOG; COG4108; Bacteria.
DR HOGENOM; CLU_002794_2_1_9; -.
DR OMA; GFVFKIH; -.
DR BioCyc; LACI272621:G1G49-661-MON; -.
DR Proteomes; UP000006381; 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;
KW Reference proteome.
FT CHAIN 1..523
FT /note="Peptide chain release factor 3"
FT /id="PRO_0000242184"
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; 59365 MW; 39C88A1F33F129C2 CRC64;
MDKELAEKVE KRRTFAIISH PDAGKTTITE QMLLFGGVIR KAGTVKARKT GNFATSDWME
IEKKRGISVT SSVMQFEYKG KRINILDTPG HQDFSEDTYR TLMAVDSAVM VIDSAKGIEP
QTKKLFKVVK QRGIPIFTFM NKLDRDGRPP LDLIAELEDL LGIEGVAMNW PIGSGQTLKG
LYDIANNRVE LYRKDGEDRF LPLNDDGTLP DSEALSQDPQ FKDTLDEIEL IKEAGNKFNR
EKIAMGDQTP VFFGSALTNF GVETFLNSFV DLAPAPESHT VNEDEELSPE DPEFSGFVFK
IQANMNPNHR DRIAFVRIGS GEFKKGLDVT LARTGKPIRL NNATEFMSSE RVQVSDAVAG
DIVGLYDTGN FQIGDSIYSG KRKIVYPALP EFTPELFMRV TAKNVMKQKS FHKGMNQLVQ
EGAIQLYRNY QTDEYILGAV GQLQFEVFQF RMKNEYNSEV EMNSIGHRVA RWIDPEQLDP
QMSNSRNLLV KDRYGNPLFL FENEFAERFF RDKYPDIKLT EKL