ID   RF2_HELP2               Reviewed;         363 AA.
AC   B6JPR7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   25-MAY-2022, entry version 63.
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=HPP12_0168;
OS   Helicobacter pylori (strain P12).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=570508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P12;
RA   Fischer W., Windhager L., Karnholz A., Zeiller M., Zimmer R., Haas R.;
RT   "The complete genome sequence of Helicobacter pylori strain P12.";
RL   Submitted (OCT-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; CP001217; ACJ07328.1; -; Genomic_DNA.
DR   RefSeq; WP_000371084.1; NC_011498.1.
DR   AlphaFoldDB; B6JPR7; -.
DR   SMR; B6JPR7; -.
DR   EnsemblBacteria; ACJ07328; ACJ07328; HPP12_0168.
DR   KEGG; hpp:HPP12_0168; -.
DR   HOGENOM; CLU_036856_6_0_7; -.
DR   OMA; YVFHPYQ; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000008198; 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..363
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000093540"
FT   MOD_RES         251
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   363 AA;  41382 MW;  04C34A912414EC35 CRC64;
     MDNYTYSELL KSLQNKCDNI ALIIKPEKIK QELERIEKEQ EDPNFWQDVL KARDTNKEKV
     RLNRLLETYQ KTKDSLDESV ELFELAQNDN DEVTLSLLYE EAPTLEHSVQ KVEIEIMLSG
     ENDASNAIIT IQPGAGGTES QDWASILYRM YLRWAERRGF KSEILDYQDG EEAGIKGVAF
     IIKGENAYGY LKNENGVHRL VRISPFDANA KRHTSFASVQ ISPELDDDID IEIDEKDVRY
     DYYRASGAGG QHVNKTESAV RITHFPTGIV VQCQNDRSQH KNKASALKML KSKLYELELE
     KQQNSTKNEE KSEIGWGHQI RSYVLAPYQQ VKDARSNIAY SNVEAILDGD IDAILEGVLI
     AKA