ID   RF2_MYCLB               Reviewed;         374 AA.
AC   B8ZUV0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, 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=MLBr00667;
OS   Mycobacterium leprae (strain Br4923).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=561304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Br4923;
RX   PubMed=19881526; DOI=10.1038/ng.477;
RA   Monot M., Honore N., Garnier T., Zidane N., Sherafi D., Paniz-Mondolfi A.,
RA   Matsuoka M., Taylor G.M., Donoghue H.D., Bouwman A., Mays S., Watson C.,
RA   Lockwood D., Khamispour A., Dowlati Y., Jianping S., Rea T.H.,
RA   Vera-Cabrera L., Stefani M.M., Banu S., Macdonald M., Sapkota B.R.,
RA   Spencer J.S., Thomas J., Harshman K., Singh P., Busso P., Gattiker A.,
RA   Rougemont J., Brennan P.J., Cole S.T.;
RT   "Comparative genomic and phylogeographic analysis of Mycobacterium
RT   leprae.";
RL   Nat. Genet. 41:1282-1289(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; FM211192; CAR70761.1; -; Genomic_DNA.
DR   RefSeq; WP_010907865.1; NC_011896.1.
DR   AlphaFoldDB; B8ZUV0; -.
DR   SMR; B8ZUV0; -.
DR   PRIDE; B8ZUV0; -.
DR   EnsemblBacteria; CAR70761; CAR70761; MLBr00667.
DR   KEGG; mlb:MLBr00667; -.
DR   HOGENOM; CLU_036856_0_1_11; -.
DR   OMA; YVFHPYQ; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000006900; 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..374
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000193555"
FT   MOD_RES         256
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   374 AA;  41872 MW;  460A95C16E24B523 CRC64;
     MEPDRQTDIA ALDSTLTTVE RVLDVEGLRT RIEKLEHEAS DPKLWDDQVR AQRVTSELSH
     AQGELRRIEE LRRRLDDLPV LYELAAEERA AAAASGMEAF AEADAELKAL RVDIEATEVR
     TLLSGEYDER EALITIRSGA GGVDAADWAE MLMRMYIRWA EQHKYGVEVL DTSYAEEAGV
     KSATFAVHAP FAYGTLASEQ GTHRLVRISP FDNQSRRQTS FAEVEVLPVV EITDHIDIPE
     GDVRVDVYRS SGPGGQSVNT TDSAVRLTHV PTGLVVTCQN EKSQLQNKVS AMRVLQAKLL
     ERKRLEERAE LDALKGRGGS SWGNQIRSYV LHPYQMVKDL RNEYEVGNPT AVLDGDIDGF
     LEAGIRWRNR RDIS