ID   RF2_STRU0               Reviewed;         366 AA.
AC   B9DRN6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 66.
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=SUB0621;
OS   Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=218495;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-854 / 0140J;
RX   PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA   Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A.,
RA   Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R.,
RA   Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D.,
RA   Parkhill J.;
RT   "Evidence for niche adaptation in the genome of the bovine pathogen
RT   Streptococcus uberis.";
RL   BMC Genomics 10:54-54(2009).
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; AM946015; CAR41450.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9DRN6; -.
DR   SMR; B9DRN6; -.
DR   STRING; 218495.SUB0621; -.
DR   PRIDE; B9DRN6; -.
DR   EnsemblBacteria; CAR41450; CAR41450; SUB0621.
DR   KEGG; sub:SUB0621; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_221244_1_0_9; -.
DR   OMA; YVFHPYQ; -.
DR   Proteomes; UP000000449; 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..366
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000193559"
FT   MOD_RES         249
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   366 AA;  41792 MW;  95CB2499284F2444 CRC64;
     MEVAEIRQKI VENKEKLTSF RRSLDLDGLE EEIALLENKM TEPDFWNDNI AAQKTSQELN
     TLKSTFETFH DMLELSDETE LYLEMLAEDE SIKEELEEAL VKLEQILSQY EMTLLLSEPY
     DHNNAILEIH PGSGGTEAQD WADMLFRMYT RFGNAKGFKV ETLDYQAGDE AGIKSVTLSF
     EGPNAYGFLK SEMGVHRLVR ISPFDSAKRR HTSFTSVEVM PELDDTIEVD IRDDDIKMDT
     FRSGGAGGQN VNKVSTGVRL THIPTGIVVA STVDRTQYGN RDRAMKMLQA KLYQLEQEKK
     AEEVNALKGD KKEITWGSQI RSYVFTPYTM VKDHRTNFEV AQVDKVMDGE IDGFIDAYLK
     WRMGDD