RF2_LISMF
ID RF2_LISMF Reviewed; 366 AA.
AC Q71WR9;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Peptide chain release factor 2;
DE Short=RF-2;
GN Name=prfB; OrderedLocusNames=LMOf2365_2482;
OS Listeria monocytogenes serotype 4b (strain F2365).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=265669;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F2365;
RX PubMed=15115801; DOI=10.1093/nar/gkh562;
RA Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA Luchansky J.B., Fraser C.M.;
RT "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT pathogen Listeria monocytogenes reveal new insights into the core genome
RT components of this species.";
RL Nucleic Acids Res. 32:2386-2395(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: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-24; 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; AE017262; AAT05247.1; -; Genomic_DNA.
DR AlphaFoldDB; Q71WR9; -.
DR SMR; Q71WR9; -.
DR KEGG; lmf:LMOf2365_2482; -.
DR HOGENOM; CLU_221244_1_0_9; -.
DR OMA; YVFHPYQ; -.
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..366
FT /note="Peptide chain release factor 2"
FT /id="PRO_0000166828"
FT MOD_RES 251
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 366 AA; 42126 MW; 64A2B05ECD547E8B CRC64;
MELAEIRNEL EKTAQQIKDF RGSLDLDSME VRIAELEDQM LDPNFWNDQQ AAQKVINESN
GYKETYQAFH ALEEEQESME ISLELLKEEA DEDLQEELEK DIKAYMATIS EFELKLMLSD
PYDKNNAILE LHPGAGGTES QDWGSMLLRM YQRWSEKKGF KVEMLDYQAG DEAGIKSVTL
LIKGHNAYGY LKAEKGVHRL VRISPFDSSG RRHTSFVSVD VMPELDDDIE IEVRTEDLKI
DTYRATGAGG QHINTTDSAV RMTHIPSGIV VTCQSERSQL KNREQAMKML KTKLYQKEQE
EKERELAEIR GEQKEIGWGS QIRSYVFHPY SMVKDHRTNY ETGNIQAVMD GDLDEFINAY
LRSRIG