RF2_ECOL6
ID RF2_ECOL6 Reviewed; 365 AA.
AC P66023; Q8XD56;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 95.
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=c5622;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN81919.1; -; Genomic_DNA.
DR RefSeq; WP_001701073.1; NC_004431.1.
DR AlphaFoldDB; P66023; -.
DR SMR; P66023; -.
DR STRING; 199310.c5622; -.
DR EnsemblBacteria; AAN81919; AAN81919; c5622.
DR GeneID; 67415224; -.
DR KEGG; ecc:c5622; -.
DR eggNOG; COG1186; Bacteria.
DR HOGENOM; CLU_220733_1_0_6; -.
DR OMA; YVFHPYQ; -.
DR Proteomes; UP000001410; 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_0000166817"
FT MOD_RES 252
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ SEQUENCE 365 AA; 41221 MW; 0B99802FDDF5A762 CRC64;
MFEINPVNNR IQDLTERSDV LRGYLDYDAK KERLEEVNAE LEQPDVWNEP ERAQALGKER
SSLEAVVDTL DQMKQGLEDV SGLLELAVEA DDEETFNEAV AELDALEEKL AQLEFRRMFS
GEYDSADCYL DIQAGSGGTE AQDWASMLER MYLRWAESRG FKTEIIEESE GEVAGIKSVT
IKISGDYAYG WLRTETGVHR LVRKSPFDSG GRRHTSFSSA FVYPEVDDDI DIEINPADLR
IDVYRASGAG GQHVNRTESA VRITHIPTGI VTQCQNDRSQ HKNKDQAMKQ MKAKLYELEM
QKKNAEKQAM EDNKSDIGWG SQIRSYVLDD SRIKDLRTGV ETRNTQAVLD GSLDQFIEAS
LKAGL
