ID   RF2_BUCAP               Reviewed;         364 AA.
AC   P59102;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2002, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Peptide chain release factor 2;
DE            Short=RF-2;
GN   Name=prfB; OrderedLocusNames=BUsg_421;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: Methylated by PrmC. Methylation increases the termination
CC       efficiency of RF2 (By similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: The gene for this protein contains a UGA in-frame
CC       termination codon after Leu-24; a naturally occurring frameshift
CC       enables complete translation of RF-2. This provides a mechanism for the
CC       protein to regulate its own production (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000305}.
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DR   EMBL; AE013218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P59102; -.
DR   SMR; P59102; -.
DR   OMA; YVFHPYQ; -.
DR   Proteomes; UP000000416; 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; Ribosomal frameshifting.
FT   CHAIN           1..364
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_0000166806"
FT   MOD_RES         251
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   364 AA;  42400 MW;  3F12ED6E88DB9A05 CRC64;
     MEINIITNKI NKLIQRKKDL KRYLDYVAKS TRILEIDLEL SSTEIWKKKE YVHNLNKEKN
     LLNIIINKIN NIEKNIKEMI IFLDLAIETK DNAIIQEISE EIKKIAEKIQ ELEFYRMFSN
     QHDHCNCYID VQAGSGGVDA QDWSKILLRM YLKWSDKKGF KTEIIEESTG EIVGIKSSTI
     KVSGQYAFGW LRTETGIHRL IRKSPFDSGK RRHTSFSSIF IYPDIEDKIN IEINPSDLRI
     DVYRASGAGG QHVNRTESAV RITHLPTNIV TQCQNNRSQH KNKEQAIKQM KSKLYEMKIK
     EKKEKQKKIE KNKSDISWGN QIRSYILDNS KIKDLRTGVE KYNVQSVLDG DLDDFIEQSL
     IMGL