ID   RF3_LACLA               Reviewed;         523 AA.
AC   Q9CIK7;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Peptide chain release factor 3;
DE            Short=RF-3;
GN   Name=prfC; OrderedLocusNames=LL0349; ORFNames=L0369;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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; AE005176; AAK04447.1; -; Genomic_DNA.
DR   PIR; E86668; E86668.
DR   RefSeq; NP_266505.1; NC_002662.1.
DR   RefSeq; WP_003131635.1; NC_002662.1.
DR   AlphaFoldDB; Q9CIK7; -.
DR   SMR; Q9CIK7; -.
DR   STRING; 272623.L0369; -.
DR   PaxDb; Q9CIK7; -.
DR   EnsemblBacteria; AAK04447; AAK04447; L0369.
DR   KEGG; lla:L0369; -.
DR   PATRIC; fig|272623.7.peg.382; -.
DR   eggNOG; COG4108; Bacteria.
DR   HOGENOM; CLU_002794_2_1_9; -.
DR   OMA; GFVFKIH; -.
DR   Proteomes; UP000002196; 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..523
FT                   /note="Peptide chain release factor 3"
FT                   /id="PRO_0000210945"
FT   DOMAIN          8..275
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"
SQ   SEQUENCE   523 AA;  59503 MW;  258B74A77C8C1952 CRC64;
     MTLQEEIKKR RTFAIISHPD AGKTTITEQL LKFGGAIREA GTVKARKTGN FAKSDWMDIE
     KERGISVTSS VMQFDYAGKR VNILDTPGHE DFSEDTYRTL MAVDAAVMVI DSAKGIEAQT
     KKLFQVVKRR GIPVFTFINK LDRDGREPLD LLSELEEILG IASVPMNWPI GMGKNFQGLY
     DFTHGRVEVY QPEDGKRFVE FDENGEVPAS HPLTKNPFFT QALEDAELLL DAGNQFSEEE
     VVAGQLTPVF FGSALTSFGV ETFLETFLEY APEPHSHKTV DEEEIEPLNP DFSGFIFKIQ
     ANMDPRHRDR IAFVRIVSGE FERGMDVNLI RTGKKVKLSN VTQFMAESRE NVENAVAGDI
     IGVYDTGTYQ VGDTLTTGKL KKSFEPLPTF TPELFMRVQA KNVMKQKSFQ KGIDQLVQEG
     AIQLYKSYTT GDIMLGAVGQ LQFEVFKDRM EREYNSETIM TPMGTKTVRW IKEEDLDEKM
     SSSRNILARD RFDHPLFLFE NEFAMRWFKD KYPDVELMEQ FSV