RF1_CAMJE
ID RF1_CAMJE Reviewed; 355 AA.
AC Q9PM63; Q0P816;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=Cj1612;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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; AL111168; CAL35709.1; -; Genomic_DNA.
DR PIR; B81257; B81257.
DR RefSeq; WP_002851189.1; NC_002163.1.
DR RefSeq; YP_002344981.1; NC_002163.1.
DR AlphaFoldDB; Q9PM63; -.
DR SMR; Q9PM63; -.
DR IntAct; Q9PM63; 6.
DR STRING; 192222.Cj1612; -.
DR PaxDb; Q9PM63; -.
DR PRIDE; Q9PM63; -.
DR EnsemblBacteria; CAL35709; CAL35709; Cj1612.
DR GeneID; 905879; -.
DR KEGG; cje:Cj1612; -.
DR PATRIC; fig|192222.6.peg.1588; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_7; -.
DR OMA; ISDHRVG; -.
DR Proteomes; UP000000799; 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; Reference proteome.
FT CHAIN 1..355
FT /note="Peptide chain release factor 1"
FT /id="PRO_0000177651"
FT REGION 280..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 231
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 355 AA; 39943 MW; 647F0202CB20B1B3 CRC64;
MLASKLDPFF KRFEELNSLL SSSDILNDIS KMTTLSKEQK NLEPIVLKAK EYLKTLDNIE
ENKALLNDPE LGELAKEELK TLEELKPKLE EEIKILLLPK DPNDERNIFL EIRAGTGGDE
ASLFVGDLVK AYARYAENRG YKLEIVSSSE GSVGGFKEII MLVKGTGAYS RLKYEGGTHR
VQRVPQTESQ GRVHTSAITV AVMPEVDDIE IEINPNDLKV DVMRSSGHGG QSVNTTDSAV
RITHIPTGIV VVNQDGKSQH KNKESAMKVL KARLYEMQES ERLAKESEAR KSQVGSGDRS
ERIRTYNFPQ NRISDHRINL TLYRLDAIMQ DGLFDEIIEP LITHHQAQAL QEQNL
