RF2_BORBU
ID RF2_BORBU Reviewed; 358 AA.
AC O51101;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 3.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Peptide chain release factor 2;
DE Short=RF-2;
GN Name=prfB; OrderedLocusNames=BB_0074;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
RN [2]
RP SEQUENCE REVISION.
RA Mongodin E.F., Fraser-Liggett C.M., Qiu W.-G., Dunn J.J., Luft B.J.,
RA Schutzer S.E., Casjens S.R.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Methylated by PrmC. Methylation increases the termination
CC efficiency of RF2 (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: The gene for this protein contains a UGA in-frame
CC termination codon after Leu-19; 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:0000305}.
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DR EMBL; AE000783; AAC66459.2; -; Genomic_DNA.
DR PIR; B70109; B70109.
DR RefSeq; NP_212208.2; NC_001318.1.
DR AlphaFoldDB; O51101; -.
DR SMR; O51101; -.
DR STRING; 224326.BB_0074; -.
DR PRIDE; O51101; -.
DR EnsemblBacteria; AAC66459; AAC66459; BB_0074.
DR KEGG; bbu:BB_0074; -.
DR PATRIC; fig|224326.49.peg.472; -.
DR HOGENOM; CLU_222237_0_0_12; -.
DR Proteomes; UP000001807; 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;
KW Ribosomal frameshifting.
FT CHAIN 1..358
FT /note="Peptide chain release factor 2"
FT /id="PRO_0000166804"
FT MOD_RES 242
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 358 AA; 41652 MW; F97C3E786B646F25 CRC64;
MKEKINTLLK HAEDIWRKLC KNEIQAKIEK YEKEINQKNF WNDPKRAQKV IKAQSILKNK
IDPWEELINK IKDLSDLCEI AENEKDTNGL EIEFNTLEKQ YKDLLTISYF KEELDANNAF
LTIHSGAGGT EACDWVAMLY RMYSRYAERK KYKTELIDLL EAEGGIKSVT IEIKGEYAYG
LLKSEVGIHR LIRISPFDAA KKRHTSFASV FVDPVIDDKI EITIKPEDIR IDTYRASGAG
GQHVNKTSSA VRITHIETGI VTQSQSDRSQ HKNKDLAMKV LKSRLYEYYK SKEDEKNKSK
QDTKKEISWG NQIRSYVFQP YNLVKDHRTK FENSNTTSVM DGNIDNFIEE YLKWKSLN