ID   RF2_BURP0               Reviewed;         367 AA.
AC   A3NX26;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 3.
DT   03-AUG-2022, entry version 81.
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};
GN   OrderedLocusNames=BURPS1106A_2644;
OS   Burkholderia pseudomallei (strain 1106a).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=357348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1106a;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
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; CP000572; ABN92528.3; -; Genomic_DNA.
DR   RefSeq; WP_004199566.1; NC_009076.1.
DR   AlphaFoldDB; A3NX26; -.
DR   SMR; A3NX26; -.
DR   EnsemblBacteria; ABN92528; ABN92528; BURPS1106A_2644.
DR   GeneID; 56596074; -.
DR   KEGG; bpl:BURPS1106A_2644; -.
DR   HOGENOM; CLU_220733_0_0_4; -.
DR   Proteomes; UP000006738; Chromosome I.
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..367
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000093534"
FT   MOD_RES         254
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   367 AA;  41091 MW;  32D2BDF5CD7AE448 CRC64;
     MEAERLNAIE SSLADLRRRA GELRGYLDYD VKSERLAEVN KQLEDPNVWN DSKNAQALGR
     EKKSLESVVT TLTALDNDLR DAQDLFELAH EEGDEETLVA TESDAAKLEA RVADIEFRRM
     FSNPADPNNC FIDIQAGAGG TEACDWASML LRQYLRYCER KGFKAEVLEE SDGDVAGIKN
     ATIKVSGEYA YGYLRTETGI HRLVRKSPFD SSGGRHTSFS SVFVYPEIDD SIEVEINPAD
     LRIDTYRASG AGGQHINKTD SAVRITHMPT GIVVQCQNDR SQHRNRAEAM AMLKSRLFEA
     ELRKRQAEQD KLESSKTDVG WGHQIRSYVL DQSRVKDLRT NVEMSNTKAV LDGDLDDFIS
     ASLKQGV