ID   RF2_MYCUA               Reviewed;         371 AA.
AC   A0PQZ6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=MUL_2412;
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=362242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99;
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA   Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA   Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
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; CP000325; ABL04765.1; -; Genomic_DNA.
DR   RefSeq; WP_011740380.1; NC_008611.1.
DR   AlphaFoldDB; A0PQZ6; -.
DR   SMR; A0PQZ6; -.
DR   STRING; 362242.MUL_2412; -.
DR   EnsemblBacteria; ABL04765; ABL04765; MUL_2412.
DR   KEGG; mul:MUL_2412; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_6_0_11; -.
DR   OMA; YVFHPYQ; -.
DR   Proteomes; UP000000765; 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.
FT   CHAIN           1..371
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000005003"
FT   MOD_RES         253
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   371 AA;  41555 MW;  29B141501528A849 CRC64;
     MEPDRQAEIA ALDSALTTVE RVLDVEGLRS RIEKLEHEAS DPKLWDDQTR AQRVTSELSH
     TQGELRRVEE LRRRLEDLPV LYELAAEEEG AAAGEALTEA DAEFKALRAD IEATEVRTLL
     SGEYDEREAL VTIRSGAGGV DAADWAEMLM RMYVRWAEQH KYPVEVFDTS YAEEAGIKSA
     TFAVHAPFAY GTLSVEQGTH RLVRISPFDN QSRRQTSFAE VEVLPVVETT DHIDIPEGDV
     RVDVYRSSGP GGQSVNTTDS AVRLTHIPTG IVVTCQNEKS QLQNKVAAMR VLQAKLLERK
     RIEERAELDA LKGDGGSSWG NQMRSYVLHP YQMVKDLRTE YEVGNPATVL DGDIDGFLEA
     GIRWRNRKDD D