ID   RF2_TREPA               Reviewed;         368 AA.
AC   O83585;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=Peptide chain release factor 2;
DE            Short=RF-2;
GN   Name=prfB; OrderedLocusNames=TP_0576;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(1998).
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; AE000520; AAC65552.1; -; Genomic_DNA.
DR   PIR; F71306; F71306.
DR   RefSeq; WP_010882022.1; NC_021490.2.
DR   AlphaFoldDB; O83585; -.
DR   SMR; O83585; -.
DR   IntAct; O83585; 1.
DR   STRING; 243276.TPANIC_0576; -.
DR   EnsemblBacteria; AAC65552; AAC65552; TP_0576.
DR   KEGG; tpa:TP_0576; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_036856_6_0_12; -.
DR   OMA; YVFHPYQ; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000000811; 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..368
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_0000166855"
FT   MOD_RES         245
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   368 AA;  41596 MW;  B8CBE848BE674A4E CRC64;
     MVHKSPPSRR ACRKYGGVFD VAAYEARIAT LEAAAAAPDF WSERARAEAL LAELKTLRAT
     LEPWRALRRE SADLRALYEL AREAQDASLE PELSSLFSDI SARFEEASLT RLLHEEVDRL
     DAFVTIHSGA GGVEACDWAQ MLMRMYTRWA ERRSFCVHIV DLLESEGGVK SVTLKICGSH
     AFGFLKGETG VHRLVRISPF DSAARRHTSF TSTYVFPVLD DHVEVHIRSE DMRVDTYRSG
     GAGGQHVNKT DSAVRITHLP TGIVVTCQNE RSQISNRATA LSLLRARLYA YERQKKQQEH
     QRFASEKKDI SWGNQIRSYV FHPYTMVKDH RSKCETGNIH AVMDGALEPF IRSYLEFLCT
     STQCVEPQ