RF2_SALTY
ID RF2_SALTY Reviewed; 365 AA.
AC P0A289; P28353;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Peptide chain release factor 2;
DE Short=RF-2;
GN Name=prfB; OrderedLocusNames=STM3041;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=2236050; DOI=10.1073/pnas.87.21.8432;
RA Kawakami K., Nakamura Y.;
RT "Autogenous suppression of an opal mutation in the gene encoding peptide
RT chain release factor 2.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:8432-8436(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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-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.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL21916.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M38590; AAA72914.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21916.1; ALT_FRAME; Genomic_DNA.
DR PIR; A36480; A36480.
DR RefSeq; NP_461957.3; NC_003197.2.
DR AlphaFoldDB; P0A289; -.
DR SMR; P0A289; -.
DR STRING; 99287.STM3041; -.
DR PaxDb; P0A289; -.
DR EnsemblBacteria; AAL21916; AAL21916; STM3041.
DR GeneID; 1254564; -.
DR KEGG; stm:STM3041; -.
DR HOGENOM; CLU_036856_6_1_6; -.
DR OMA; YVFHPYQ; -.
DR PhylomeDB; P0A289; -.
DR Proteomes; UP000001014; 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..365
FT /note="Peptide chain release factor 2"
FT /id="PRO_0000166843"
FT MOD_RES 252
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 365 AA; 41149 MW; BAA868A07BFF219C CRC64;
MFEINPVNNR IQDLTERTNV LRGYLDYDAK KERLEEVNAE LEQPDVWNEP ERAQALGKER
SSLEAIVDTL DQMTQGLDDV SGLLELAVEA DDEETFNEAV AELNTLEEKL AQLEFRRMFS
GEYDSADCYL DIQAGSGGTE AQDWASMLLR MYLRWAEARG FKTEVIEESE GEVAGIKSAT
IKISGEYAYG WLRTETGVHR LVRKSPFDSG GRRHTSFSSA FVYPEVDDDI DIDINPADLR
IDVYRASGAG GQHVNRTESA VRITHIPTGI VTQCQNDRSQ HKNKDQAMKQ MKAKLYELEM
QKKNAEKQAM EDTKSDIGWG SQIRSYVLDD SRIKDLRTGV ETRNTQAVLD GSLDQFIEAS
LKAGL