RF2_CAMJE
ID RF2_CAMJE Reviewed; 365 AA.
AC Q9PMK5; Q0P8G0;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Peptide chain release factor 2 {ECO:0000255|HAMAP-Rule:MF_00094};
DE Short=RF-2 {ECO:0000255|HAMAP-Rule:MF_00094};
GN Name=prfB {ECO:0000255|HAMAP-Rule:MF_00094}; OrderedLocusNames=Cj1455;
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 2 directs the termination of
CC translation in response to the peptide chain termination codons UGA and
CC UAA. {ECO:0000255|HAMAP-Rule:MF_00094}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00094}.
CC -!- PTM: Methylated by PrmC. Methylation increases the termination
CC efficiency of RF2. {ECO:0000255|HAMAP-Rule:MF_00094}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000255|HAMAP-Rule:MF_00094}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL111168; CAL35563.1; -; Genomic_DNA.
DR PIR; F81291; F81291.
DR RefSeq; WP_002851475.1; NC_002163.1.
DR RefSeq; YP_002344837.1; NC_002163.1.
DR AlphaFoldDB; Q9PMK5; -.
DR SMR; Q9PMK5; -.
DR IntAct; Q9PMK5; 8.
DR STRING; 192222.Cj1455; -.
DR PaxDb; Q9PMK5; -.
DR PRIDE; Q9PMK5; -.
DR EnsemblBacteria; CAL35563; CAL35563; Cj1455.
DR GeneID; 905743; -.
DR KEGG; cje:Cj1455; -.
DR PATRIC; fig|192222.6.peg.1435; -.
DR eggNOG; COG1186; Bacteria.
DR HOGENOM; CLU_036856_6_0_7; -.
DR OMA; YVFHPYQ; -.
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_00094; Rel_fac_2; 1.
DR InterPro; IPR005139; PCRF.
DR InterPro; IPR000352; Pep_chain_release_fac_I.
DR InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR InterPro; IPR004374; PrfB.
DR Pfam; PF03462; PCRF; 1.
DR Pfam; PF00472; RF-1; 1.
DR SMART; SM00937; PCRF; 1.
DR SUPFAM; SSF75620; SSF75620; 1.
DR TIGRFAMs; TIGR00020; prfB; 1.
DR PROSITE; PS00745; RF_PROK_I; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methylation; Protein biosynthesis; Reference proteome.
FT CHAIN 1..365
FT /note="Peptide chain release factor 2"
FT /id="PRO_0000166808"
FT MOD_RES 251
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ SEQUENCE 365 AA; 41068 MW; 6B95FD027D44921B CRC64;
MDNYEFSELL KTLKNKVGNI ASIIKPENIQ TRLKEIEELE NSPSFWSDVK QAGIIGKEKT
KITNLLKNYE NAFNALNDAS ELFDLANSEN DTETLEALFN DAPKLEDTIT SLEISMLLSG
ENDGKNAIVS IHPGAGGTES NDWASILYRM YLRFCEREGF KVETLDFQEG EEAGLKDVSF
LVKGENAYGY LKAENGIHRL VRTSPFDSAG RRHTSFSSVM VSPELDDDIE IEIEEKDIRI
DYYRASGAGG QHVNKTESAV RITHFPTGIV VQCQNDRSQH KNKATAFKML KSRLYELELM
KQQDSANTGE KSEIGWGHQI RSYVLFPYQQ VKDNRSGEAF SQVDNILDGD IKKMIEGVLI
ALKAE
