RF2_MYCLE
ID RF2_MYCLE Reviewed; 374 AA.
AC O32885;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Peptide chain release factor 2;
DE Short=RF-2;
GN Name=prfB; OrderedLocusNames=ML0667; ORFNames=MLCB1779.24c;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Methylated by PrmC. Methylation increases the termination
CC efficiency of RF2 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000305}.
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DR EMBL; Z98271; CAB11005.1; -; Genomic_DNA.
DR EMBL; AL583919; CAC30176.1; -; Genomic_DNA.
DR PIR; T45313; T45313.
DR RefSeq; NP_301541.1; NC_002677.1.
DR RefSeq; WP_010907865.1; NC_002677.1.
DR AlphaFoldDB; O32885; -.
DR SMR; O32885; -.
DR STRING; 272631.ML0667; -.
DR EnsemblBacteria; CAC30176; CAC30176; CAC30176.
DR KEGG; mle:ML0667; -.
DR PATRIC; fig|272631.5.peg.1188; -.
DR Leproma; ML0667; -.
DR eggNOG; COG1186; Bacteria.
DR HOGENOM; CLU_036856_0_1_11; -.
DR OMA; YVFHPYQ; -.
DR Proteomes; UP000000806; 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..374
FT /note="Peptide chain release factor 2"
FT /id="PRO_0000166831"
FT MOD_RES 256
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 374 AA; 41872 MW; 460A95C16E24B523 CRC64;
MEPDRQTDIA ALDSTLTTVE RVLDVEGLRT RIEKLEHEAS DPKLWDDQVR AQRVTSELSH
AQGELRRIEE LRRRLDDLPV LYELAAEERA AAAASGMEAF AEADAELKAL RVDIEATEVR
TLLSGEYDER EALITIRSGA GGVDAADWAE MLMRMYIRWA EQHKYGVEVL DTSYAEEAGV
KSATFAVHAP FAYGTLASEQ GTHRLVRISP FDNQSRRQTS FAEVEVLPVV EITDHIDIPE
GDVRVDVYRS SGPGGQSVNT TDSAVRLTHV PTGLVVTCQN EKSQLQNKVS AMRVLQAKLL
ERKRLEERAE LDALKGRGGS SWGNQIRSYV LHPYQMVKDL RNEYEVGNPT AVLDGDIDGF
LEAGIRWRNR RDIS