RF2_BURMA
ID RF2_BURMA Reviewed; 367 AA.
AC Q62J00;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=BMA1699;
OS Burkholderia mallei (strain ATCC 23344).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=243160;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23344;
RX PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT "Structural flexibility in the Burkholderia mallei genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
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 -!- MISCELLANEOUS: The gene for this protein contains a UGA in-frame
CC termination codon after Leu-27; a naturally occurring frameshift
CC enables complete translation of RF-2. This provides a mechanism for the
CC protein to regulate its own production (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000255|HAMAP-Rule:MF_00094}.
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DR EMBL; CP000010; AAU47810.1; -; Genomic_DNA.
DR RefSeq; WP_004199566.1; NC_006348.1.
DR RefSeq; YP_103319.1; NC_006348.1.
DR AlphaFoldDB; Q62J00; -.
DR SMR; Q62J00; -.
DR STRING; 243160.BMA1699; -.
DR EnsemblBacteria; AAU47810; AAU47810; BMA1699.
DR GeneID; 56596074; -.
DR KEGG; bma:BMA1699; -.
DR PATRIC; fig|243160.12.peg.1740; -.
DR eggNOG; COG1186; Bacteria.
DR HOGENOM; CLU_220733_0_0_4; -.
DR OMA; YVFHPYQ; -.
DR Proteomes; UP000006693; Chromosome 1.
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; Ribosomal frameshifting.
FT CHAIN 1..367
FT /note="Peptide chain release factor 2"
FT /id="PRO_1000004976"
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
