ID   RF2_SYNY3               Reviewed;         372 AA.
AC   P74476;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   25-MAY-2022, entry version 133.
DE   RecName: Full=Peptide chain release factor 2;
DE            Short=RF-2;
GN   Name=prfB; OrderedLocusNames=sll1865;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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   -!- MISCELLANEOUS: The gene for this protein contains a UGA in-frame
CC       termination codon after Leu-26; a naturally occurring frameshift
CC       enables complete translation of RF-2. This provides a mechanism for the
CC       protein to regulate its own production (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000305}.
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DR   EMBL; BA000022; BAA18577.1; ALT_SEQ; Genomic_DNA.
DR   PIR; S76448; S76448.
DR   AlphaFoldDB; P74476; -.
DR   SMR; P74476; -.
DR   IntAct; P74476; 2.
DR   STRING; 1148.1653665; -.
DR   PaxDb; P74476; -.
DR   EnsemblBacteria; BAA18577; BAA18577; BAA18577.
DR   KEGG; syn:sll1865; -.
DR   eggNOG; COG1186; Bacteria.
DR   InParanoid; P74476; -.
DR   OMA; YVFHPYQ; -.
DR   PhylomeDB; P74476; -.
DR   Proteomes; UP000001425; 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;
KW   Ribosomal frameshifting.
FT   CHAIN           1..372
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_0000166853"
FT   MOD_RES         254
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   372 AA;  41760 MW;  6D09A365E17A0A6D CRC64;
     MITELTDLKR NLELISSRLG QTQDYLDLPG LKAKVQDLEQ CAAQPDFWDD TDQAQQILQT
     LNETKSQLEQ WGIWQQQWQD SQAIVELLEL EDDQALLTEA ETTLEQLQKE LDRWELQQLL
     SGPYDAKGAT LTINAGAGGT DAQDWAEMLL RMYTRWSEKQ GYKVHLAEIS EGDEAGLKSV
     TLEIEGRYAY GYLKSEKGTH RLVRISPFNA NGKRQTSFAG VEVMPLLGEE AISLDIPDKD
     LDISTSRAGG KGGQNVNKVE TAVRIVHLPT GLAVRCTQER SQLQNKEKAL AILKAKLLIV
     LEEQRAQAIA EIRGDMVEAA WGTQIRNYVF HPYQLVKDLR TNVETTDVGG VMDGELSDFI
     EAYLRHSARL DS