RF2_YERE8
ID RF2_YERE8 Reviewed; 365 AA.
AC A1JPL5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=YE3376;
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081;
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(2006).
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-25; 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; AM286415; CAL13403.1; -; Genomic_DNA.
DR RefSeq; WP_011817019.1; NC_008800.1.
DR RefSeq; YP_001007546.1; NC_008800.1.
DR AlphaFoldDB; A1JPL5; -.
DR SMR; A1JPL5; -.
DR STRING; 393305.YE3376; -.
DR EnsemblBacteria; CAL13403; CAL13403; YE3376.
DR KEGG; yen:YE3376; -.
DR PATRIC; fig|393305.7.peg.3583; -.
DR eggNOG; COG1186; Bacteria.
DR HOGENOM; CLU_220733_1_0_6; -.
DR OMA; YVFHPYQ; -.
DR Proteomes; UP000000642; 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; Ribosomal frameshifting.
FT CHAIN 1..365
FT /note="Peptide chain release factor 2"
FT /id="PRO_1000005023"
FT MOD_RES 252
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ SEQUENCE 365 AA; 41172 MW; 6B892C18F8D37939 CRC64;
MFEINPVKNR IQDLSDRTAV LRGYLDYDAK KERLEEVNAE LEQPDVWNEP ERAQALGKER
SSLEEIVTTI DQLDQGMDDV TGLLELAIEA DDEETFNEAV AELDILDGKL GQLEFRRMFS
GEYDSANCYL DLQAGSGGTE AQDWASMLLR MYLRWAEAKG FKTEIIEESD GDVAGLKSAT
IKIIGDYAFG WLRTETGVHR LVRKSPFDSG GRRHTSFSSA FVYPEVDDDI DIEINPADLR
IDVYRASGAG GQHVNKTESA VRITHIPTNI VTQCQNDRSQ HKNKDQAMKQ LKAKLYEFEM
QKKNADKQML EDNKSDIGWG SQIRSYVLDD SRIKDLRTGV ETRNTQAVLD GDLDKFIEAS
LKAGL
