ID   RF2_LACLM               Reviewed;         365 AA.
AC   A2RLF5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=llmg_1547;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
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; AM406671; CAL98122.1; -; Genomic_DNA.
DR   RefSeq; WP_011835386.1; NZ_WJVF01000002.1.
DR   AlphaFoldDB; A2RLF5; -.
DR   SMR; A2RLF5; -.
DR   STRING; 416870.llmg_1547; -.
DR   EnsemblBacteria; CAL98122; CAL98122; llmg_1547.
DR   KEGG; llm:llmg_1547; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_036856_6_0_9; -.
DR   OMA; YVFHPYQ; -.
DR   PhylomeDB; A2RLF5; -.
DR   BioCyc; LLAC416870:LLMG_RS07780-MON; -.
DR   Proteomes; UP000000364; 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_1000004992"
FT   MOD_RES         251
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   365 AA;  41547 MW;  20C524630650352F CRC64;
     MELSEIRNLL EGYSEKINGF RDSLDLDRLE EEIALLENDM AQPEFWNDQA AAQKVIDESN
     ALKAKYDNYQ AMNTMLEEAQ TMLEMLQEEA DEDMQVELEE MTTALGQKIE SYELEIMLNQ
     PYDHMNAVLE IHPGSGGTES QDWGSMLMRM YTRWGEAHGF KVEILDYQDG DVAGLKSVAI
     RFVGRNAYGF LRGEKGVHRL VRISPFDSAN RRHTSFTSVD VMPELDDSIE VEVRDADVKM
     DTFRSGGAGG QNVNKVSTGV RLTHVPTGIV VQSTMDRTQY GNRDKAMAML KSKLYQLEMD
     KKQAEVDELR GDQSEISWGS QIRSYVFMPY QLVKDTRTGY ETGQISNVMD GEIDGFINAY
     LRWNL