ID   RF1_HELPJ               Reviewed;         352 AA.
AC   Q9ZMZ0;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Peptide chain release factor 1;
DE            Short=RF-1;
GN   Name=prfA; OrderedLocusNames=jhp_0072;
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 1 directs the termination of
CC       translation in response to the peptide chain termination codons UAG and
CC       UAA. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: Methylated by PrmC. Methylation increases the termination
CC       efficiency of RF1 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000305}.
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DR   EMBL; AE001439; AAD05656.1; -; Genomic_DNA.
DR   PIR; F71977; F71977.
DR   RefSeq; WP_000025168.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZMZ0; -.
DR   SMR; Q9ZMZ0; -.
DR   STRING; 85963.jhp_0072; -.
DR   EnsemblBacteria; AAD05656; AAD05656; jhp_0072.
DR   KEGG; hpj:jhp_0072; -.
DR   PATRIC; fig|85963.30.peg.962; -.
DR   eggNOG; COG0216; Bacteria.
DR   OMA; ISDHRVG; -.
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_00093; Rel_fac_1; 1.
DR   InterPro; IPR005139; PCRF.
DR   InterPro; IPR000352; Pep_chain_release_fac_I.
DR   InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR   InterPro; IPR004373; RF-1.
DR   Pfam; PF03462; PCRF; 1.
DR   Pfam; PF00472; RF-1; 1.
DR   SMART; SM00937; PCRF; 1.
DR   SUPFAM; SSF75620; SSF75620; 1.
DR   TIGRFAMs; TIGR00019; prfA; 1.
DR   PROSITE; PS00745; RF_PROK_I; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methylation; Protein biosynthesis.
FT   CHAIN           1..352
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000177682"
FT   REGION          288..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         233
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   352 AA;  39586 MW;  05B98C4F759BDE47 CRC64;
     MSILAEKLSS ILKRYDELTA LLSSVEVVSD IKKLTELSKE QSSIEEISVA SKEYLSVLEG
     IKENKELLED KELSELAKEE LKILEIQKSE LETAIKQLLI PKDPNDDKNI YLELRAGTGG
     DEAGIFVGDL FKAYCRYADL KKWKVEIVSS SENSVGGYKE IIVLIKGKGV YSRLKFEAGT
     HRVQRVPETE SQGRIHTSAI TVAIMPEVDD VEVSINPSDL KIEVFRAGGH GGQCVNTTDS
     AVRITHLPTN ISVSMQDEKS QHKNKDKALK ILKARLYEKQ IEEQQLANAK DRKEQVGSGD
     RSERIRTYNY PQNRLSEHRI NLTLYSLEEI MLSGNLDEVI NPLIAHAQSQ FE