ID   RF2_THEMA               Reviewed;         369 AA.
AC   Q9X1R5;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=Peptide chain release factor 2;
DE            Short=RF-2;
GN   Name=prfB; OrderedLocusNames=TM_1579;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
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   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000305}.
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DR   EMBL; AE000512; AAD36646.1; -; Genomic_DNA.
DR   PIR; D72238; D72238.
DR   RefSeq; NP_229379.1; NC_000853.1.
DR   AlphaFoldDB; Q9X1R5; -.
DR   SMR; Q9X1R5; -.
DR   STRING; 243274.THEMA_06385; -.
DR   EnsemblBacteria; AAD36646; AAD36646; TM_1579.
DR   KEGG; tma:TM1579; -.
DR   PATRIC; fig|243274.5.peg.1598; -.
DR   eggNOG; COG1186; Bacteria.
DR   InParanoid; Q9X1R5; -.
DR   OMA; YVFHPYQ; -.
DR   Proteomes; UP000008183; 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..369
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_0000166854"
FT   MOD_RES         251
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   369 AA;  42637 MW;  BE41E95ED6A4FACB CRC64;
     MGMISFETKT KIEELEKKYK DVLSVVNEDE INKELEEVEK KLTDPSVWDD QKKAREYTQK
     LKRLKNISED LKRVRSLFED LEVAIELSDE DQEMAQHVEE IVQELEGAVK KLELEIILNG
     KYDPNNAYLS VHPGAGGTES QDWAQMLLRM YMRWAERKGF DVEIVEFQPG EEAGIKDATI
     LIKGEYAYGY LKHESGVHRL VRISPFDAAR RRHTSFASVN VIPEIDDDVD IEIRPEDLKI
     ETFRASGHGG QYVNKTESAV RITHLPTGIV VSCQNERSQH QNKQTALKIL KAKLYQLEME
     KKRREIQEIQ GELKDISWGN QIRSYIFHPY TMVKDHRTGV ETANVDAVMD GDIDMFIEAE
     LVYFARRSS