ID   RF2_BUCBP               Reviewed;         366 AA.
AC   Q89AC4;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Peptide chain release factor 2;
DE            Short=RF-2;
GN   Name=prfB; OrderedLocusNames=bbp_390;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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-26; 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; AE016826; AAO27102.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q89AC4; -.
DR   SMR; Q89AC4; -.
DR   STRING; 224915.bbp_390; -.
DR   EnsemblBacteria; AAO27102; AAO27102; bbp_390.
DR   KEGG; bab:bbp_390; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_036856_6_0_6; -.
DR   OMA; YVFHPYQ; -.
DR   Proteomes; UP000000601; 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;
KW   Ribosomal frameshifting.
FT   CHAIN           1..366
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_0000166807"
FT   MOD_RES         253
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   366 AA;  42338 MW;  15F9B2960628D09C CRC64;
     MFKNNNIIND RITNLVSQIN KLKRRLDYDI KKNRLLEINM ELKLPETWKH PSLIKKINKE
     KNQLISVVTQ ITKIDNDVQE LIDILNLENS NNINSILDNV LYEFKNIEKS IHELEKCSMF
     LGKYDYLSCY VDIQSGSGGV EAQDWASMLL RMYVRWAESK KFKIDIIEQT YGEVVGIKSA
     TIEVLGKYAF GWFRTETGIH RLVRKSPFNA HHRRHTSFSS VYVYPILDDA INVDINTRDL
     KIDVYRASGA GGQHVNKTES AVRIRHLPTG IVVQCQNDRS QHKNKDQAMK QLKAKLYEQL
     INEKKCQQKI LENNKLNIGW GHQIRSYTLD NSRIKDLRTG VESKNIQSVL DGGLDLFVEC
     SLRNGL