ID   RF2_STRGC               Reviewed;         364 AA.
AC   A8AY61;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Peptide chain release factor 2 {ECO:0000255|HAMAP-Rule:MF_00094};
DE            Short=RF-2 {ECO:0000255|HAMAP-Rule:MF_00094};
GN   Name=prfB {ECO:0000255|HAMAP-Rule:MF_00094}; OrderedLocusNames=SGO_1441;
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).
CC   -!- FUNCTION: Peptide chain release factor 2 directs the termination of
CC       translation in response to the peptide chain termination codons UGA and
CC       UAA. {ECO:0000255|HAMAP-Rule:MF_00094}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00094}.
CC   -!- PTM: Methylated by PrmC. Methylation increases the termination
CC       efficiency of RF2. {ECO:0000255|HAMAP-Rule:MF_00094}.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000255|HAMAP-Rule:MF_00094}.
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DR   EMBL; CP000725; ABV09192.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8AY61; -.
DR   SMR; A8AY61; -.
DR   STRING; 467705.SGO_1441; -.
DR   PRIDE; A8AY61; -.
DR   EnsemblBacteria; ABV09192; ABV09192; SGO_1441.
DR   KEGG; sgo:SGO_1441; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_221244_1_0_9; -.
DR   OMA; YVFHPYQ; -.
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_00094; Rel_fac_2; 1.
DR   InterPro; IPR005139; PCRF.
DR   InterPro; IPR000352; Pep_chain_release_fac_I.
DR   InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR   InterPro; IPR004374; PrfB.
DR   Pfam; PF03462; PCRF; 1.
DR   Pfam; PF00472; RF-1; 1.
DR   SMART; SM00937; PCRF; 1.
DR   SUPFAM; SSF75620; SSF75620; 1.
DR   TIGRFAMs; TIGR00020; prfB; 1.
DR   PROSITE; PS00745; RF_PROK_I; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methylation; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..364
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000075531"
FT   MOD_RES         249
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   364 AA;  41504 MW;  A3F0ED687F61F99A CRC64;
     MDISEIRQKI DANREKLASF RGSLDLEGLE EEIAILENKM TEPDFWDDNI AAQKTSQELN
     ELKQTYENFH QMTDLFDESE ILLDFLAEDD SVQEELEEKL AELEKMMTSY EMTLLLSEPY
     DNNNAILEIH PGSGGTEAQD WGDMLLRMYT RFGNAKGFKV EVLDYQAGDE AGIKSVTLSF
     EGPHAYGLLK SEMGVHRLVR ISPFDSAKRR HTSFTSVEVM PELDDTIEVE IREDDIKMDT
     FRSGGAGGQN VNKVSTGVRL THIPTGIVVQ STVDRTQYGN RDRAMKMLQA KLYQLEQEKK
     AAEVDSLKGD KKEISWGSQI RSYVFTPYTM VKDHRTSYEV AQVDKVMDGD LDGFIDAYLK
     WRLN