ID   RF2_HELPJ               Reviewed;         363 AA.
AC   Q9ZMR1;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Peptide chain release factor 2;
DE            Short=RF-2;
GN   Name=prfB; OrderedLocusNames=jhp_0157;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: Methylated by PrmC. Methylation increases the termination
CC       efficiency of RF2 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000305}.
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DR   EMBL; AE001439; AAD05740.1; -; Genomic_DNA.
DR   PIR; F71966; F71966.
DR   RefSeq; WP_000371078.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZMR1; -.
DR   SMR; Q9ZMR1; -.
DR   STRING; 85963.jhp_0157; -.
DR   EnsemblBacteria; AAD05740; AAD05740; jhp_0157.
DR   KEGG; hpj:jhp_0157; -.
DR   PATRIC; fig|85963.30.peg.865; -.
DR   eggNOG; COG1186; Bacteria.
DR   OMA; YVFHPYQ; -.
DR   Proteomes; UP000000804; 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_0000166822"
FT   MOD_RES         251
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   363 AA;  41329 MW;  5B0D08DE6B49CE2B CRC64;
     MDNYTYSELL KSLQNKCDNI ALIIKPEKIK QELERIEKEQ EDPNFWQDVL KARDTNKEKV
     RLNRLLETYQ KMKNSLDESV ELFELAQNDS DEVTLSLLYE EAPTLEHSVQ KVEIEIMLSG
     ENDASNAIIT IQPGAGGTES QDWASILYRM YLRWAERKSF KSEILDYQDG EEAGIKGVAF
     IIKGENAYGY LKNENGVHRL VRISPFDANA KRHTSFASVQ ISPELDDDID IEIDEKDVRY
     DYYRASGAGG QHVNKTESAV RITHFPTGIV VQCQNDRSQH KNKASALKML KSKLYELELE
     KQQSSAKNEE KSEIGWGHQI RSYVLAPYQQ VKDARSNIAY SNVEAILDGD IDAILEGVLI
     AKA