ID   RF1_LEPBP               Reviewed;         353 AA.
AC   B0SQV0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=LEPBI_I3282;
OS   Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=456481;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Patoc 1 / ATCC 23582 / Paris;
RX   PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA   Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA   Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA   Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA   Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT   "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT   into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL   PLoS ONE 3:E1607-E1607(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; CP000786; ABZ99347.1; -; Genomic_DNA.
DR   RefSeq; WP_012390203.1; NC_010602.1.
DR   AlphaFoldDB; B0SQV0; -.
DR   SMR; B0SQV0; -.
DR   STRING; 456481.LEPBI_I3282; -.
DR   KEGG; lbi:LEPBI_I3282; -.
DR   HOGENOM; CLU_036856_0_1_12; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   BioCyc; LBIF456481:LEPBI_RS16075-MON; -.
DR   Proteomes; UP000001847; Chromosome I.
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; Reference proteome.
FT   CHAIN           1..353
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000093471"
FT   MOD_RES         230
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   353 AA;  39502 MW;  0471ACBC8439A205 CRC64;
     MIDRLKKIQE KYLRIEDELA KATASDTLKN LSKERSRLTP VYTKADEYLK ITKDCQDAKS
     LLESENDPDM HSMLKSEIEE GEKKLEELAK ELEIMLLPPD PNSGKSILVE IRAGTGGEES
     GLFCADLFRM YNKYADKKGL RVEIIDMSQT GIGGYKEIVF SLDDDKAYDL FKFESGTHRV
     QRIPETESGG RIHTSAVTVA ILPEAEEKEV EIKESDLRID VYRSSGAGGQ HVNTTDSAVR
     ITHIPTGIVV ASQEERSQIK NRDKAMRVLR ARIADQAAET AKLSADALKK AQVGSGDRSE
     RIRTYNFPQG RCTDHRIGFT SHNLPAIMEG DLDELIDALI QEDRSKRLAE AKA