ID   RF2_MYCMM               Reviewed;         371 AA.
AC   B2HGJ2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 69.
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=MMAR_1527;
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=216594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M;
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
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; CP000854; ACC39978.1; -; Genomic_DNA.
DR   RefSeq; WP_012393367.1; NC_010612.1.
DR   AlphaFoldDB; B2HGJ2; -.
DR   SMR; B2HGJ2; -.
DR   STRING; 216594.MMAR_1527; -.
DR   EnsemblBacteria; ACC39978; ACC39978; MMAR_1527.
DR   GeneID; 64260224; -.
DR   KEGG; mmi:MMAR_1527; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_6_0_11; -.
DR   OMA; YVFHPYQ; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000001190; 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..371
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000093547"
FT   MOD_RES         253
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   371 AA;  41525 MW;  29B7F63B6527F8BC CRC64;
     MEPDRQAEIA ALDSALTTVE RVLDVEGLRS RIEKLEHEAS DPKLWDDQTR AQRVTSELSH
     TQGELRRVEE LRRRLEDLPV LYELAAEEEG AAAGEALAEA 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