ID   RF2_CAMFF               Reviewed;         369 AA.
AC   A0RQM7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=CFF8240_1369;
OS   Campylobacter fetus subsp. fetus (strain 82-40).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=82-40;
RA   Fouts D.E., Nelson K.E.;
RT   "Sequence of Campylobacter fetus subsp. fetus 82-40.";
RL   Submitted (NOV-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; CP000487; ABK83126.1; -; Genomic_DNA.
DR   RefSeq; WP_011732174.1; NC_008599.1.
DR   AlphaFoldDB; A0RQM7; -.
DR   SMR; A0RQM7; -.
DR   STRING; 360106.CFF8240_1369; -.
DR   EnsemblBacteria; ABK83126; ABK83126; CFF8240_1369.
DR   GeneID; 61065185; -.
DR   KEGG; cff:CFF8240_1369; -.
DR   PATRIC; fig|360106.6.peg.1332; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_036856_6_0_7; -.
DR   OMA; NKPDLWD; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000000760; 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..369
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000004979"
FT   MOD_RES         251
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   369 AA;  41999 MW;  EB99CBD099193C2F CRC64;
     MDSYEYTELL KKLNTKVQNI SRVIKPQDIE IRLKEIEDIE NRPEFWNDIK KASEIGKEKT
     KISNMLCKFK NVKSAISDAY ELYELANAED DEQTINSLFE DAQNLENKIT NLEISMMLSG
     EDDSKNAIVS IHPGAGGTES NDWASMLYRM YLRFCEREGF KVETLDFQEG DEAGLKDVSF
     IVKGENAYGY LKAENGIHRL VRTSPFDSAG RRHTSFSSVM VSPEVDDDIA IEIEEKDLRL
     DYYRASGAGG QHVNKTESAV RITHIPTGIV VQCQNDRSQH KNKATAMKML KSRLYEFELM
     KQQEANNAIE KSEIGWGHQI RSYVLFPYQQ VKDTRSGEAY SQTDAILDGD IKKIIESVLI
     SQKSSANKE