ID   RF2_STRGG               Reviewed;         368 AA.
AC   B1VV08;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=SGR_4555;
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350;
RX   PubMed=18375553; DOI=10.1128/jb.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT   griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
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; AP009493; BAG21384.1; -; Genomic_DNA.
DR   RefSeq; WP_003968784.1; NC_010572.1.
DR   AlphaFoldDB; B1VV08; -.
DR   SMR; B1VV08; -.
DR   STRING; 455632.SGR_4555; -.
DR   EnsemblBacteria; BAG21384; BAG21384; SGR_4555.
DR   GeneID; 6211951; -.
DR   KEGG; sgr:SGR_4555; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_036856_6_0_11; -.
DR   OMA; YVFHPYQ; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000001685; 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.
FT   CHAIN           1..368
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000093557"
FT   MOD_RES         251
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   368 AA;  40811 MW;  37469C7A1783B589 CRC64;
     MAVVDISEEL KSLSSTMGSI EAVLDLDALR ADIAALEEQA AAPSLWDDPE AAQKITSKLS
     HLQAEVRKAE TLRGRIDDLE VLFELAADEG DADAQAEAEA ELESVRKALD EMEVRTLLSG
     EYDAREALVT IRAEAGGVDA ADFAEKLQRM YLRWAEQHNY KTEVYETAYA EEAGIKSTTF
     AVQVPYAYGT LSVEQGTHRL VRISPFDNQG RRQTSFAGVE VLPVVEQTDH IEIDESELRV
     DVYRSSGPGG QGVNTTDSAV RLTHLPTGIV VSCQNERSQI QNKASAMNVL QAKLLERRRQ
     EEQAKMNALK GDGGNSWGNQ MRSYVLHPYQ MVKDLRTEFE MGNPEAVFNG EIDGFVEAGI
     RWRKQSEK