ID   RF1_TREPS               Reviewed;         351 AA.
AC   B2S1Z9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=TPASS_0051;
OS   Treponema pallidum subsp. pallidum (strain SS14).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=455434;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS14;
RX   PubMed=18482458; DOI=10.1186/1471-2180-8-76;
RA   Matejkova P., Strouhal M., Smajs D., Norris S.J., Palzkill T.,
RA   Petrosino J.F., Sodergren E., Norton J.E., Singh J., Richmond T.A.,
RA   Molla M.N., Albert T.J., Weinstock G.M.;
RT   "Complete genome sequence of Treponema pallidum ssp. pallidum strain SS14
RT   determined with oligonucleotide arrays.";
RL   BMC Microbiol. 8:76-76(2008).
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; CP000805; ACD70478.1; -; Genomic_DNA.
DR   RefSeq; WP_012460512.1; NC_021508.1.
DR   AlphaFoldDB; B2S1Z9; -.
DR   SMR; B2S1Z9; -.
DR   EnsemblBacteria; ACD70478; ACD70478; TPASS_0051.
DR   GeneID; 57878592; -.
DR   KEGG; tpp:TPASS_0051; -.
DR   PATRIC; fig|455434.6.peg.48; -.
DR   OMA; ISDHRVG; -.
DR   Proteomes; UP000001202; 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..351
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000093519"
FT   MOD_RES         233
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   351 AA;  40205 MW;  A693C6F953B5797C CRC64;
     MIEKLEELRA QWRKLQQEVE NPSLFSSTQS YRERMRDHAY LSRLMEEYDR YLLTEKQLED
     AHVLIQDESD ADFKDVIRQE IRTLEAALHT SQKRLKTLLI PPDPLQEKNI IMEIRGGTGG
     DEAALFAADL FRMYTHYAES KQWRYEVLAV SETELGGFKE ITFSISGRDV YGSLRYESGV
     HRVQRVPSTE ASGRIHTSAV TVAVLPEMEE TEVDIRAEDV RVDVMRASGP GGQCVNTTDS
     AVRLTHLPTG IVVVCQDEKS QIKNKAKAMR VLRSRVYDLE ESKRQVARAR ERKSQVGSGD
     RSERIRTYNF PQNRVTDHRV RVTLYKLDAV MQGALDDIIE PLCIASRESV I