RF1_BORAP
ID RF1_BORAP Reviewed; 357 AA.
AC Q0SNW8; G0IR39;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 92.
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};
GN OrderedLocusNames=BAPKO_0198, BafPKo_0192;
OS Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=390236;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PKo;
RX PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J.,
RA Wilske B., Platzer M.;
RT "Comparative genome analysis: selection pressure on the Borrelia vls
RT cassettes is essential for infectivity.";
RL BMC Genomics 7:211-211(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PKo;
RX PubMed=22123755; DOI=10.1128/jb.05951-11;
RA Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J.,
RA Fraser-Liggett C.M., Schutzer S.E.;
RT "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT Lyme disease agent isolates.";
RL J. Bacteriol. 193:6995-6996(2011).
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; CP000395; ABH01460.1; -; Genomic_DNA.
DR EMBL; CP002933; AEL69425.1; -; Genomic_DNA.
DR RefSeq; WP_011600883.1; NC_017238.1.
DR AlphaFoldDB; Q0SNW8; -.
DR SMR; Q0SNW8; -.
DR STRING; 390236.BafPKo_0192; -.
DR EnsemblBacteria; AEL69425; AEL69425; BafPKo_0192.
DR KEGG; baf:BAPKO_0198; -.
DR KEGG; bafz:BafPKo_0192; -.
DR PATRIC; fig|390236.22.peg.191; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_12; -.
DR OMA; ISDHRVG; -.
DR OrthoDB; 928964at2; -.
DR Proteomes; UP000005216; 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..357
FT /note="Peptide chain release factor 1"
FT /id="PRO_0000263241"
FT REGION 282..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 234
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 357 AA; 41692 MW; 652B0F69C2C6EB6D CRC64;
MFLEKLNSAT SRIKSIEEKL QDINLIKNQK KYSKIIKEYT YLEKINTKKI EYENILNQIN
DNKTILEKEE QQEMKELIKQ ELIDLDKKKE NLEHEIKILL LPQDENDSKN IIIEIRAGTG
GEEAALFANN LYSMYIKYSE KKKWKTEIIN FNETELGGFK EIIFEIKGKD VFKKLKYESG
VHRVQRIPIT ESNGRLQTSA ATVAVLPNIE ETEIDINEKD LRIDVYRSSG AGGQHVNTTD
SAVRITHLPT GIVVQCQNER SQHKNKDQAM KILRARLYEF EDSKKQEQRS NNRKQQVGSG
DRSERIRTYN FPQNRITDHR ANITLYKLEE FMQGELDQLL DPLTIELQEQ TLKSNNI
