ID   RF2_BUCAI               Reviewed;         365 AA.
AC   P57511; Q9F454;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   04-MAY-2001, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Peptide chain release factor 2;
DE            Short=RF-2;
GN   Name=prfB; OrderedLocusNames=BU436;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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-25; 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; BA000003; BAB13134.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; NP_240248.1; NC_002528.1.
DR   AlphaFoldDB; P57511; -.
DR   SMR; P57511; -.
DR   STRING; 107806.10039100; -.
DR   EnsemblBacteria; BAB13134; BAB13134; BAB13134.
DR   KEGG; buc:BU436; -.
DR   PATRIC; fig|107806.10.peg.445; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_036856_6_0_6; -.
DR   OMA; YVFHPYQ; -.
DR   Proteomes; UP000001806; 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..365
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_0000166805"
FT   MOD_RES         252
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   365 AA;  42799 MW;  96B8BDA8BA49973F CRC64;
     MIENNMTTNQ INSLNRRVQD LKRYLDYNKK KSRVLEIDLE LSSPKTWTEQ ISIKKLNKEK
     YLLNSIIQNI NEIEENIKEV VIFLELAIET QDNLVFKESL LEIQKIEQEI KKLEFYRMFS
     KKNDHYDCYI DIQSGSGGTD AQDWSKMLLR MYLRWADKKG FHTEIIDESI GEIVGIKSST
     IKVSGEYAFG WFRTETGIHR LIRKSPFDSG KRRHTSFSSI FIYPDINEKI DININYSDLR
     IDVYRASGAG GQHVNRTESA VRITHLPTNI VTQCQNNRSQ HKNKEQAMKQ MQSKLYEIQM
     RKKQEEKQKI EQNKSDITWG NQIRSYILDN SKIKDLRTGV EKNHVQSVLD GDLDDFIEQS
     LIMGL