ID   RF2_RENSM               Reviewed;         374 AA.
AC   A9WPT6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=RSal33209_1356;
OS   Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS   NBRC 15589 / NCIMB 2235).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Renibacterium.
OX   NCBI_TaxID=288705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235;
RX   PubMed=18723615; DOI=10.1128/jb.00721-08;
RA   Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA   Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA   Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT   "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT   reductive evolution away from an environmental Arthrobacter ancestor.";
RL   J. Bacteriol. 190:6970-6982(2008).
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; CP000910; ABY23093.1; -; Genomic_DNA.
DR   RefSeq; WP_012244774.1; NC_010168.1.
DR   AlphaFoldDB; A9WPT6; -.
DR   SMR; A9WPT6; -.
DR   STRING; 288705.RSal33209_1356; -.
DR   PRIDE; A9WPT6; -.
DR   EnsemblBacteria; ABY23093; ABY23093; RSal33209_1356.
DR   KEGG; rsa:RSal33209_1356; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_036856_6_0_11; -.
DR   OMA; YVFHPYQ; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000002007; 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_1000093553"
FT   MOD_RES         254
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   374 AA;  41298 MW;  AB38AA4B747D5D22 CRC64;
     MADIDFPAEL RALRALRATY DSIERVIDAD SLRKDIAVLS EQAGVPDLWD NPAEAQKVTS
     KLSHAQSKLE RLETLTARID DLEVLVELAE SEHDEDSLAE ASKELVSLQK SLQELEVVTL
     LAGEYDEREA VVTIRSGAGG VDAADFAEML LRMYLRWAER HGYPTSVLDT SYAEEAGLKS
     ATFEVKAPYA FGTLSVEAGT HRLVRISPFD NQGRRQTSFA AVEVIPLIEQ TDSIEIPDND
     IRVDVFRSSG PGGQSVNTTD SAVRLTHLPT GTVVSMQNEK SQLQNRAAAT RVLQSRLLLL
     KKQQEDAEKK ALAGDVKASW GDQMRSYVLN PYQMVKDLRT EHEVGNTSGV LDGDIDDFID
     AGIRWRANNR NAAE