ID   RF2_CAMJJ               Reviewed;         365 AA.
AC   A1W163;
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};
GN   OrderedLocusNames=CJJ81176_1448;
OS   Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=354242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81-176;
RA   Fouts D.E., Nelson K.E., Sebastian Y.;
RL   Submitted (DEC-2006) 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; CP000538; EAQ72778.1; -; Genomic_DNA.
DR   RefSeq; WP_002869186.1; NC_008787.1.
DR   AlphaFoldDB; A1W163; -.
DR   SMR; A1W163; -.
DR   STRING; 354242.CJJ81176_1448; -.
DR   EnsemblBacteria; EAQ72778; EAQ72778; CJJ81176_1448.
DR   KEGG; cjj:CJJ81176_1448; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_036856_6_0_7; -.
DR   OMA; YVFHPYQ; -.
DR   Proteomes; UP000000646; 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.
FT   CHAIN           1..365
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000004981"
FT   MOD_RES         251
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   365 AA;  41085 MW;  51AE9886A443C943 CRC64;
     MDNYEFSELL KTLKNKVGNI ASIIKPENIQ TRLKEIEELE NSPSFWSDVK QAGIIGKEKT
     KITNLLKNYE NAFNALNDAN ELFDLANSEN DTETLEALFN DASKLEDTIT SLEISMLLSG
     ENDGKNAIVS IHPGAGGTES NDWASILYRM YLRFCEREGF KVETLDFQEG EEAGLKDVSF
     LVKGENAYGY LKAENGIHRL VRTSPFDSAG RRHTSFSSVM VSPELDDDIE IEIEEKDIRI
     DYYRASGAGG QHVNKTESAV RITHFPTGIV VQCQNDRSQH KNKATAFKML KSRLYELELM
     KQQDSANTGE KSEIGWGHQI RSYVLFPYQQ VKDNRSGEAF SQVDNILDGD IKKMIEGVLI
     ALKAE