RF2_CAMJD
ID RF2_CAMJD Reviewed; 365 AA.
AC A7H5G4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
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};
GN OrderedLocusNames=JJD26997_1790;
OS Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 /
OS 269.97).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1458 / RM4099 / 269.97;
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT "Complete genome sequence of Campylobacter jejuni subsp doylei 269.97
RT isolated from human blood.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000768; ABS44503.1; -; Genomic_DNA.
DR AlphaFoldDB; A7H5G4; -.
DR SMR; A7H5G4; -.
DR EnsemblBacteria; ABS44503; ABS44503; JJD26997_1790.
DR KEGG; cjd:JJD26997_1790; -.
DR HOGENOM; CLU_036856_6_0_7; -.
DR OMA; YVFHPYQ; -.
DR Proteomes; UP000002302; 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.
FT CHAIN 1..365
FT /note="Peptide chain release factor 2"
FT /id="PRO_1000004980"
FT MOD_RES 251
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ SEQUENCE 365 AA; 41121 MW; AD2C16F2BB6DCD29 CRC64;
MDNYEFSELL KTLKNKVGNI ASIIKPKNIQ TRLKEIEELE NSPSFWNDVK QAGIIGKEKT
KITNLLKNYE NAFNALNDAS ELFDLANSEN DIETLQALFN DAPKLEDTIT SLEISMLLSG
ENDGKNAIVS IHPGAGGTES NDWASILYRM YLRFCEREGF KVETLDFQEG EEAGLKDVSF
LVKGENAYGY LKAENGIHRL VRTSPFDSAG RRHTSFSSVM VSPELDDDIE IEIEEKDIRI
DYYRASGAGG QHVNKTESAV RITHFPTGIV VQCQNDRSQH KNKATAFKML KSRLYELELM
KQQDSANSSE KSEIGWGHQI RSYVLFPYQQ VKDNRSGEAF SQVDNILDGD IKKMIEGVLI
ALKAE