ID   RF2_LACLA               Reviewed;         365 AA.
AC   Q9CGX1;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 108.
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=LL0971;
GN   ORFNames=L0374;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(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: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; AE005176; AAK05069.1; -; Genomic_DNA.
DR   PIR; C86746; C86746.
DR   RefSeq; NP_267127.1; NC_002662.1.
DR   RefSeq; WP_003130963.1; NC_002662.1.
DR   AlphaFoldDB; Q9CGX1; -.
DR   SMR; Q9CGX1; -.
DR   STRING; 272623.L0374; -.
DR   PaxDb; Q9CGX1; -.
DR   EnsemblBacteria; AAK05069; AAK05069; L0374.
DR   GeneID; 60356401; -.
DR   GeneID; 66441937; -.
DR   KEGG; lla:L0374; -.
DR   PATRIC; fig|272623.7.peg.1039; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_036856_6_0_9; -.
DR   OMA; YVFHPYQ; -.
DR   Proteomes; UP000002196; 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..365
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_0000166823"
FT   MOD_RES         251
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   365 AA;  41570 MW;  2E0DE00653E995C9 CRC64;
     MELSEIRNLL EGYAEKINGF RESLDLERLE EEIALLENDM AQPEFWNDQA AAQKVIDESN
     ALKAKYDNYQ AMNNMLEEAQ TMLEMLQEEA DEEMQAELEE MTIALGQKIE SYELEIMLNQ
     PYDHMNAVLE IHPGSGGTES QDWGSMLMRM YTRWGEAHGF KVEILDYQDG DVAGLKSVAL
     RFVGRNAYGF LRGEKGVHRL VRISPFDSAN RRHTSFTSVD VMPELDDSIE VDVRDADVKM
     DTFRSGGAGG QNVNKVSTGV RLTHIPTGIV VQSTMDRTQY GNRDKAMAML KSKLYQLEMD
     KKQAEVDELR GDQSEISWGS QIRSYVFMPY QLVKDTRTGY ETGQISNVMD GELDGFINAY
     LRWNL