ID   RF2_THEAB               Reviewed;         369 AA.
AC   B7IE81;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=THA_1882;
OS   Thermosipho africanus (strain TCF52B).
OC   Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; Thermosipho.
OX   NCBI_TaxID=484019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TCF52B;
RX   PubMed=19124572; DOI=10.1128/jb.01448-08;
RA   Nesboe C.L., Bapteste E., Curtis B., Dahle H., Lopez P., Macleod D.,
RA   Dlutek M., Bowman S., Zhaxybayeva O., Birkeland N.-K., Doolittle W.F.;
RT   "The genome of Thermosipho africanus TCF52B: lateral genetic connections to
RT   the Firmicutes and Archaea.";
RL   J. Bacteriol. 191:1974-1978(2009).
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; CP001185; ACJ76308.1; -; Genomic_DNA.
DR   RefSeq; WP_004102881.1; NC_011653.1.
DR   AlphaFoldDB; B7IE81; -.
DR   SMR; B7IE81; -.
DR   STRING; 484019.THA_1882; -.
DR   PRIDE; B7IE81; -.
DR   EnsemblBacteria; ACJ76308; ACJ76308; THA_1882.
DR   KEGG; taf:THA_1882; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_036856_6_0_0; -.
DR   OMA; YVFHPYQ; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000002453; 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..369
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000117264"
FT   MOD_RES         249
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   369 AA;  42845 MW;  D1BC7C0573CB195B CRC64;
     MIDFELKQKI DEAKKKFEDI IKVFHPENKR KELEELEKQM GDSDFWSDQR KAREISQKAQ
     RIRKIIDDMK DIEAKFEDLD AAIELSDEDQ SFVETIKEMV EEIEKKVKTF ELELILNGKF
     DASNAYLTIH PGAGGTESQD WASMLLRMYM RWAERKGFDV QIVDYQPGEE AGIKSAMIYI
     KGDYAYGYLK YERGVHRLVR ISPFDANKRR HTSFASVNVI PEIDDDIDIE INPEDLRIDT
     YRASGAGGQY VNKTESAVRI THIPTGIVVT CQTERSQLQN KETALKVLKA RLYQLELEKR
     QKQLEEIQGE LKDISWGNQI RSYVFQPYTM VKDHRTNVET GNIDAVMDGE IDIFIESELI
     HFAGIRNKQ