ID F9VBI1_LACGL Unreviewed; 523 AA.
AC F9VBI1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Peptide chain release factor 3 {ECO:0000256|HAMAP-Rule:MF_00072};
DE Short=RF-3 {ECO:0000256|HAMAP-Rule:MF_00072};
GN Name=prfC {ECO:0000256|HAMAP-Rule:MF_00072};
GN OrderedLocusNames=LCGL_0222 {ECO:0000313|EMBL:BAK59682.1};
OS Lactococcus garvieae (strain Lg2) (Enterococcus seriolicida).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=420890 {ECO:0000313|EMBL:BAK59682.1, ECO:0000313|Proteomes:UP000008520};
RN [1] {ECO:0000313|EMBL:BAK59682.1, ECO:0000313|Proteomes:UP000008520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lg2 {ECO:0000313|EMBL:BAK59682.1,
RC ECO:0000313|Proteomes:UP000008520};
RX PubMed=21829716; DOI=10.1371/journal.pone.0023184;
RA Morita H., Toh H., Oshima K., Yoshizaki M., Kawanishi M., Nakaya K.,
RA Suzuki T., Miyauchi E., Ishii Y., Tanabe S., Murakami M., Hattori M.;
RT "Complete genome sequence and comparative analysis of the fish pathogen
RT Lactococcus garvieae.";
RL PLoS ONE 6:E23184-E23184(2011).
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:0000256|HAMAP-Rule:MF_00072}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|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:0000256|ARBA:ARBA00009978, ECO:0000256|HAMAP-Rule:MF_00072}.
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DR EMBL; AP009333; BAK59682.1; -; Genomic_DNA.
DR RefSeq; WP_014024214.1; NC_017490.1.
DR AlphaFoldDB; F9VBI1; -.
DR STRING; 420890.LCGL_0222; -.
DR KEGG; lgv:LCGL_0222; -.
DR PATRIC; fig|420890.5.peg.219; -.
DR eggNOG; COG4108; Bacteria.
DR HOGENOM; CLU_002794_2_1_9; -.
DR Proteomes; UP000008520; 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.70.3280; Peptide chain release factor 3, domain III; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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 NCBIfam; TIGR00503; prfC; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43556; PEPTIDE CHAIN RELEASE FACTOR RF3; 1.
DR PANTHER; PTHR43556:SF2; PEPTIDE CHAIN RELEASE FACTOR RF3; 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; SSF54980; EF-G C-terminal domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00072};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00072};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00072}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00072};
KW Reference proteome {ECO:0000313|Proteomes:UP000008520}.
FT DOMAIN 8..275
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT BINDING 85..89
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT BINDING 139..142
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
SQ SEQUENCE 523 AA; 59498 MW; 77529177DF64E08A CRC64;
MNRAEEIKKR RTFAIISHPD AGKTTITEQL LKFGGAIREA GTVKARKTGN FAKSDWMDIE
KERGISVTSS VMQFDYAGKR VNILDTPGHE DFSEDTYRTL MAVDAAVMVI DSAKGIEAQT
KKLFQVVKRR GIPVFTFINK LDRDGREPLD LLSELEDILG IASVPMNWPI GMGKNFQGLY
DFYNKRIEVY QPENGQRFIE FGENGEIDAS HPLTSNPFYA QAMEDAELLL DAGNEFDEEE
VLAGQLTPVF FGSALTDFGV ETFLDTFLTY APEPNGHKTI EDEIIDPLRE EFSGFVFKIQ
ANMDIRHRDR IAFVRIVSGE FERGMGVKLL RTGKQVKLSN VTQFMAESRE NVENAVAGDI
IGVYDTGTYQ VGDTLTTGKL KTPFEPLPTF TPELFMRVTA KNVMKQKSFQ KGIEQLVQEG
AIQLYKTYTT GEIMLGAVGQ LQFEVFKHRM ENEYNSEIIM TPMGSKTVRW IKPEDLDEKM
SSSRNILARD RFDHPLFLFE NDFAMRWFKD KYPDVELMEQ FSV
//
