ID   RF2_PSELT               Reviewed;         367 AA.
AC   A8F531;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=Tlet_0699;
OS   Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 /
OS   TMO) (Thermotoga lettingae).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Pseudothermotoga.
OX   NCBI_TaxID=416591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Foster B., Bruce D., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA   Richardson P.;
RT   "Complete sequence of Thermotoga lettingae TMO.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000812; ABV33265.1; -; Genomic_DNA.
DR   RefSeq; WP_012002746.1; NC_009828.1.
DR   AlphaFoldDB; A8F531; -.
DR   SMR; A8F531; -.
DR   STRING; 416591.Tlet_0699; -.
DR   EnsemblBacteria; ABV33265; ABV33265; Tlet_0699.
DR   KEGG; tle:Tlet_0699; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_036856_6_0_0; -.
DR   OMA; YVFHPYQ; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000002016; 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..367
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000057626"
FT   MOD_RES         249
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   367 AA;  42494 MW;  5B420C569B757571 CRC64;
     MITYETRVKI DELREKYLNF VKLIDPDKLN MELKKMESEM SDPEIWKDQR KAGEISKKVR
     RIKELLSDIS EIERNFEDID VGIELSEEDP GIAQDIEKIV QEVEKNIRRF QLELILNDPL
     DQNNAYLSIH PGAGGTESHD WAQMLLRMYM RWAERKGFIV ELLDFQPGEE AGLKSATILV
     KGEYAYGYLK HERGVHRLVR ISPFDAAKRR HTSFASVNVV PEISDDIDVE IKPEDIRIDT
     FRASGHGGQY VNRTDSAVRI THLPTGIVVS CQSERSQHQN KALAMKVLKA KLYQLELAKR
     REQLDEIQGE LKEISWGNQI RSYILQPYTL VKDHRTDIET GNFDAVLDGE LDQFIEAELL
     YFADYKI