RF1_LEPBA
ID RF1_LEPBA Reviewed; 353 AA.
AC B0SH84;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=LBF_3169;
OS Leptospira biflexa serovar Patoc (strain Patoc 1 / Ames).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=355278;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Patoc 1 / Ames;
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; CP000777; ABZ95638.1; -; Genomic_DNA.
DR RefSeq; WP_012390203.1; NC_010842.1.
DR AlphaFoldDB; B0SH84; -.
DR SMR; B0SH84; -.
DR PRIDE; B0SH84; -.
DR KEGG; lbf:LBF_3169; -.
DR HOGENOM; CLU_036856_0_1_12; -.
DR OMA; ISDHRVG; -.
DR BioCyc; LBIF355278:LBF_RS16105-MON; -.
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..353
FT /note="Peptide chain release factor 1"
FT /id="PRO_1000093470"
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