ID   RF2_ECOLC               Reviewed;         365 AA.
AC   B1ITB1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=EcolC_0818;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS   WDCM 00012 / Crooks).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=481805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Ingram L., Richardson P.;
RT   "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL   Submitted (FEB-2008) 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: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   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000255|HAMAP-Rule:MF_00094}.
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DR   EMBL; CP000946; ACA76490.1; -; Genomic_DNA.
DR   RefSeq; WP_001701073.1; NZ_CP022959.1.
DR   AlphaFoldDB; B1ITB1; -.
DR   SMR; B1ITB1; -.
DR   PRIDE; B1ITB1; -.
DR   GeneID; 67415224; -.
DR   KEGG; ecl:EcolC_0818; -.
DR   HOGENOM; CLU_220733_1_0_6; -.
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.
FT   CHAIN           1..365
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000075524"
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