ID   RF2_HELPH               Reviewed;         363 AA.
AC   Q1CUY8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, 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}; OrderedLocusNames=HPAG1_0167;
OS   Helicobacter pylori (strain HPAG1).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=357544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPAG1;
RX   PubMed=16788065; DOI=10.1073/pnas.0603784103;
RA   Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A.,
RA   Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G.,
RA   Gordon J.I.;
RT   "The complete genome sequence of a chronic atrophic gastritis Helicobacter
RT   pylori strain: evolution during disease progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006).
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; CP000241; ABF84234.1; -; Genomic_DNA.
DR   RefSeq; WP_000371131.1; NC_008086.1.
DR   AlphaFoldDB; Q1CUY8; -.
DR   SMR; Q1CUY8; -.
DR   EnsemblBacteria; ABF84234; ABF84234; HPAG1_0167.
DR   KEGG; hpa:HPAG1_0167; -.
DR   HOGENOM; CLU_036856_6_0_7; -.
DR   OMA; YVFHPYQ; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000008835; 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_1000004990"
FT   MOD_RES         251
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   363 AA;  41324 MW;  5DB5EA017767D76A CRC64;
     MDNYTYSELL KSLQNKCDNI ALIIKPEKIK QELERIEKEQ EDPNFWQDVL KARDTNKEKV
     RLNRLLETYQ KTKNSLDESV ELFELAQNDN DEVTLSLLYE EAPTLEHSVQ KVEIEIMLSG
     ENDASNAIIT IQPGAGGTES QDWASILYRM YLRWAERRGF KSEILDYQDG EEAGIKGVAF
     IIKGENAYGY LKNENGVHRL VRISPFDANA KRHTSFASVQ ISPELDDDID IEIDEKDVRY
     DYYRASGAGG QHVNKTESAV RITHFPTGIV VQCQNDRSQH KNKASALKML KSKLYELELE
     KQQSSAKNEE KSEIGWGHQI RSYVLAPYQQ VKDARSNIAY SNVEAILDGD IDAILEGVLI
     AKA