RF1_STRPC
ID RF1_STRPC Reviewed; 359 AA.
AC Q1JLQ2;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 86.
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=MGAS9429_Spy0980;
OS Streptococcus pyogenes serotype M12 (strain MGAS9429).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=370551;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS9429;
RX PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA Musser J.M.;
RT "Molecular genetic anatomy of inter- and intraserotype variation in the
RT human bacterial pathogen group A Streptococcus.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
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; CP000259; ABF32167.1; -; Genomic_DNA.
DR RefSeq; WP_002989800.1; NC_008021.1.
DR AlphaFoldDB; Q1JLQ2; -.
DR SMR; Q1JLQ2; -.
DR EnsemblBacteria; ABF32167; ABF32167; MGAS9429_Spy0980.
DR KEGG; spk:MGAS9429_Spy0980; -.
DR HOGENOM; CLU_036856_0_1_9; -.
DR OMA; ISDHRVG; -.
DR PHI-base; PHI:4652; -.
DR Proteomes; UP000002433; 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..359
FT /note="Peptide chain release factor 1"
FT /id="PRO_0000263365"
FT MOD_RES 236
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 359 AA; 40600 MW; B94692766B5A7BD7 CRC64;
MNIYDQLQAV EDRYEELGEL LSDPDVVSDT KRFMELSREE ANTRETVTAY REYKQVIQTI
SDAEEMIKDA SGDPELEEMA KEELKESKAA KEEYEEKLKI LLLPKDPNDD KNIILEIRGA
AGGDEAALFA GDLLTMYQKY AETQGWRFEV MESSVNGVGG IKEVVAMVSG QSVYSKLKYE
SGAHRVQRVP VTESQGRVHT STATVLVMPE VEEVEYDIDQ KDLRVDIYHA SGAGGQNVNK
VATAVRMVHI PTGIKVEMQE ERTQQKNRDK AMKIIRARVA DHFAQIAQDE QDAERKSTVG
TGDRSERIRT YNFPQNRVTD HRIGLTLQKL DTILSGKMDE VIDALVMYDQ TKKLESLNN