ID   RF1_STRGC               Reviewed;         359 AA.
AC   P47850; A8AXD1;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=Peptide chain release factor 1;
DE            Short=RF-1;
GN   Name=prfA; OrderedLocusNames=SGO_1154;
OS   Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS   DL1 / V288).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=467705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX   PubMed=17720781; DOI=10.1128/jb.01023-07;
RA   Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT   "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT   to competence signaling peptide.";
RL   J. Bacteriol. 189:7799-7807(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67.
RX   PubMed=8598265; DOI=10.1111/j.1574-6968.1996.tb07973.x;
RA   McNab R.;
RT   "Cloning and sequence analysis of thymidine kinase from the oral bacterium
RT   Streptococcus gordonii.";
RL   FEMS Microbiol. Lett. 135:103-110(1996).
CC   -!- FUNCTION: Peptide chain release factor 1 directs the termination of
CC       translation in response to the peptide chain termination codons UAG and
CC       UAA. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: Methylated by PrmC. Methylation increases the termination
CC       efficiency of RF1 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000305}.
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DR   EMBL; CP000725; ABV10075.1; -; Genomic_DNA.
DR   EMBL; L40415; AAB02290.1; -; Genomic_DNA.
DR   RefSeq; WP_012000560.1; NC_009785.1.
DR   AlphaFoldDB; P47850; -.
DR   SMR; P47850; -.
DR   STRING; 467705.SGO_1154; -.
DR   EnsemblBacteria; ABV10075; ABV10075; SGO_1154.
DR   KEGG; sgo:SGO_1154; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_9; -.
DR   OMA; ISDHRVG; -.
DR   Proteomes; UP000001131; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00093; Rel_fac_1; 1.
DR   InterPro; IPR005139; PCRF.
DR   InterPro; IPR000352; Pep_chain_release_fac_I.
DR   InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR   InterPro; IPR004373; RF-1.
DR   Pfam; PF03462; PCRF; 1.
DR   Pfam; PF00472; RF-1; 1.
DR   SMART; SM00937; PCRF; 1.
DR   SUPFAM; SSF75620; SSF75620; 1.
DR   TIGRFAMs; TIGR00019; prfA; 1.
DR   PROSITE; PS00745; RF_PROK_I; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methylation; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..359
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000177750"
FT   REGION          288..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..303
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         236
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   359 AA;  40701 MW;  8FD3BE7270995FF0 CRC64;
     MNIYEQLQAV EDRYEELGEL LSDPDVVSDT KRFMELSKEE ASTRDTVTAY REYKQVLQNI
     VDAEEMIKES GGDADLEEMA KQELKDAKAE KEEYEEKLKI LLLPKDPNDD KNIILEIRGA
     AGGDEAQLFA GDLLQMYQKY AESQGWRFEV MEASYNGVGG IKEVVAMVSG QSVYSKLKYE
     SGAHRVQRVP VTESQGRVHT STATVLVMPE IEEVEYDIDP KDLRVDIYHA SGAGGQNVNK
     VATAVRIVHL PTNIKVEMQE ERTQQKNRDK AMKIIRARVA DHFAQIAQDE QDAERKSTIG
     TGDRSERIRT YNFPQNRVTD HRIGLTLQKL DTILAGKLDE VVDALVLYDQ TQKLEELNK