RF1_BACCZ
ID RF1_BACCZ Reviewed; 355 AA.
AC Q630R9;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 25-MAY-2022, entry version 100.
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=BCE33L5029;
OS Bacillus cereus (strain ZK / E33L).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=288681;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZK / E33L;
RX PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAU15250.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000001; AAU15250.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000887065.1; NZ_CP009968.1.
DR AlphaFoldDB; Q630R9; -.
DR SMR; Q630R9; -.
DR EnsemblBacteria; AAU15250; AAU15250; BCE33L5029.
DR GeneID; 59156823; -.
DR GeneID; 64200645; -.
DR KEGG; bcz:BCE33L5029; -.
DR PATRIC; fig|288681.22.peg.315; -.
DR Proteomes; UP000002612; 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..355
FT /note="Peptide chain release factor 1"
FT /id="PRO_0000177628"
FT MOD_RES 233
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 355 AA; 40356 MW; 40D016BA7D839382 CRC64;
MLDRLQAVEN RYEKLNELLS DPAIISDSNK LREYSKEQSD IQETVEVYRE YKDVREQLKD
AKAMLEDKLD AEMREMVKEE VSELESQEKT LSERLKILLV PKDPNDDKNV IVEVRGAAGG
DEAALFAGDL YRMYSRYAEV QGWKTEIIEA SYTELGGYKE IIFMINGKGA FAKLKFENGA
HRVQRVPETE SGGRIHTSTA TVAVLPEAEE VEIDIHEKDV RVDTFASSGP GGQSVNTTMS
AVRLTHLPTG VVVSCQDEKS QIKNKEKAMK VLRARVYDKF RQEAQAEYDQ NRKQAVGTGD
RSERIRTYNF PQNRVTDHRI GLTIQKLDQI LQGKLDDFIN ALVMEDQAQR MEAAE