ID   RF2_AQUAE               Reviewed;         373 AA.
AC   O67695;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Peptide chain release factor 2;
DE            Short=RF-2;
GN   Name=prfB; OrderedLocusNames=aq_1840;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000305}.
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DR   EMBL; AE000657; AAC07656.1; -; Genomic_DNA.
DR   PIR; E70458; E70458.
DR   RefSeq; NP_214263.1; NC_000918.1.
DR   RefSeq; WP_010881199.1; NC_000918.1.
DR   AlphaFoldDB; O67695; -.
DR   SMR; O67695; -.
DR   STRING; 224324.aq_1840; -.
DR   EnsemblBacteria; AAC07656; AAC07656; aq_1840.
DR   KEGG; aae:aq_1840; -.
DR   PATRIC; fig|224324.8.peg.1420; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_036856_6_0_0; -.
DR   InParanoid; O67695; -.
DR   OMA; YVFHPYQ; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000000798; 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..373
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_0000166800"
FT   MOD_RES         250
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   373 AA;  43309 MW;  A20146472563F326 CRC64;
     MMMVELKGKV EELRKRLEDV KKILSPEKLE SELKELDQKM SEPNFWEDQE KAKQVIQRRK
     WVEETLNKLK NLEKSVKDLE ELVEITSEED TETWAMMDEE IKEVERTLRE LELKTYLSGE
     MDAKNAYLTI QAGAGGTEAC DWADMLFRMY KRWAEKKGYE VELIDITPDD VAGIKSVTVL
     VKGPYAYGYL KGEQGVHRLV RISPFDANAR RHTSFAAVSV MPQIDEDIKI EIKPEDLKIE
     TFRASGAGGQ YVNKTDTAVR ITHIPTGITV SCQQERSQYQ NKRKALELLK AKLYQLEMKK
     LEEKKKQYEG EKTDIGWGHQ IRSYVFHPYK LIKDLRTGYE TGNVEAVMDG EIDEFIESYL
     KWKAQKEKES SNN