RF2_CORGL
ID RF2_CORGL Reviewed; 368 AA.
AC Q8NS78;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=Cgl0801, cg0913;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
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; BA000036; BAB98194.1; -; Genomic_DNA.
DR EMBL; BX927150; CAF19507.1; -; Genomic_DNA.
DR RefSeq; NP_600030.1; NC_003450.3.
DR RefSeq; WP_003863507.1; NC_006958.1.
DR AlphaFoldDB; Q8NS78; -.
DR SMR; Q8NS78; -.
DR STRING; 196627.cg0913; -.
DR KEGG; cgb:cg0913; -.
DR KEGG; cgl:Cgl0801; -.
DR PATRIC; fig|196627.13.peg.783; -.
DR eggNOG; COG1186; Bacteria.
DR HOGENOM; CLU_036856_6_0_11; -.
DR OMA; YVFHPYQ; -.
DR Proteomes; UP000000582; 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..368
FT /note="Peptide chain release factor 2"
FT /id="PRO_0000166815"
FT MOD_RES 248
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ SEQUENCE 368 AA; 41137 MW; C94D86D050AC5230 CRC64;
MRPEFSAELS ELDSTLTTIE KVLNPQEMSD RVRELEAQAA DPSLWDDPDH AQQVTSELSH
VQAELRKITD LRQRIEDLPI MVELAEEEDG DTSIAEEELA DLRSLIDALE VKTMLSGEYD
AREAVINIRS GAGGVDAADW AEMLMRMYTR WAEKNGHKVD IYDISYAEEA GIKSATFVVH
GDYMYGQLSV EQGAHRLVRI SPFDNQGRRQ TSFAEVEVLP VVEKVDSIDI PDADVRVDVY
RSSGPGGQSV NTTDSAVRLT HIPTGIVVTC QNEKSQIQNK ASAMRVLQAK LLERKRQEER
AEMDALGAGG NASWGNQMRS YVLHPYQMVK DLRTNFEVND PQKVLDGDID GLLEAGIRWR
MAESQSAE