ID   RF1_HELP2               Reviewed;         352 AA.
AC   B6JPI0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Peptide chain release factor 1 {ECO:0000255|HAMAP-Rule:MF_00093};
DE            Short=RF-1 {ECO:0000255|HAMAP-Rule:MF_00093};
GN   Name=prfA {ECO:0000255|HAMAP-Rule:MF_00093}; OrderedLocusNames=HPP12_0081;
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 1 directs the termination of
CC       translation in response to the peptide chain termination codons UAG and
CC       UAA. {ECO:0000255|HAMAP-Rule:MF_00093}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00093}.
CC   -!- PTM: Methylated by PrmC. Methylation increases the termination
CC       efficiency of RF1. {ECO:0000255|HAMAP-Rule:MF_00093}.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000255|HAMAP-Rule:MF_00093}.
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DR   EMBL; CP001217; ACJ07241.1; -; Genomic_DNA.
DR   RefSeq; WP_000025108.1; NC_011498.1.
DR   AlphaFoldDB; B6JPI0; -.
DR   SMR; B6JPI0; -.
DR   EnsemblBacteria; ACJ07241; ACJ07241; HPP12_0081.
DR   KEGG; hpp:HPP12_0081; -.
DR   HOGENOM; CLU_036856_0_1_7; -.
DR   OMA; ISDHRVG; -.
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_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_1000093461"
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:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   352 AA;  39531 MW;  0001F21F8002C163 CRC64;
     MSILAEKLSS ILKRYDELTA LLSSAEVISD IKKLTELSKE QSSIEEISIA SKEYLSVLEG
     IKENKELLED KELSELAKEE LKILEIQKSE LETAIKQLLI PKDPNDDKNI YLELRAGTGG
     DEAGIFVGDL FKAYCRYADL KKWKVEIVSS SENSVGGYKE IIALIKGKGV YSRLKFEAGT
     HRVQRVPETE SQGRIHTSAI TVAIMPEVDD VEVSINPSDL KIEVFRAGGH GGQCVNTTDS
     AVRITHLPTN ISVSMQDEKS QHKNKDKALK ILKARLYEKQ IEEQQLANAK DRKEQVGSGD
     RSERIRTYNY PQNRLSEHRI NLTLYSLEEI MLSGSLDEVI NPLIAHAQSQ FE