ID   RF2_CHLTR               Reviewed;         369 AA.
AC   O84465;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Peptide chain release factor 2;
DE            Short=RF-2;
GN   Name=prfB; OrderedLocusNames=CT_459;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(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   -!- MISCELLANEOUS: The gene for this protein contains a UGA in-frame
CC       termination codon after Leu-23; 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; AE001273; AAC68059.1; -; Genomic_DNA.
DR   PIR; G71510; G71510.
DR   RefSeq; NP_219972.1; NC_000117.1.
DR   RefSeq; WP_010725203.1; NC_000117.1.
DR   AlphaFoldDB; O84465; -.
DR   SMR; O84465; -.
DR   STRING; 813.O172_02510; -.
DR   EnsemblBacteria; AAC68059; AAC68059; CT_459.
DR   GeneID; 884235; -.
DR   KEGG; ctr:CT_459; -.
DR   PATRIC; fig|272561.5.peg.496; -.
DR   HOGENOM; CLU_221953_0_0_0; -.
DR   InParanoid; O84465; -.
DR   OMA; YVFHPYQ; -.
DR   Proteomes; UP000000431; 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..369
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_0000166813"
FT   MOD_RES         251
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   369 AA;  42608 MW;  475431B8EECFACC0 CRC64;
     MHENFDKRLE LLLEGLALTR RSLFDPEGKE NELKELEQQA VQDGFWDDVV RAGKISERIA
     RLKQQLSEFN ELKNKVSAIQ FFLEDEESSK DLEMQKELEK EFVFCEKKIT EWETLRLLSG
     ELDRNSCFLS INAGAGGTES CDWVEMLLRM YMRWASSHSW RIEVIDRLDG EVAGIKHITL
     KLVGEYAYGY AKAESGVHRL VRISPFDSNA KRHTSFASVE VFPEIDDKIE VEIRPGDIRI
     DTYRSSGAGG QHVNVTDSAV RITHFPTGIV VSCQNERSQI QNREACMNML RARIYQKLLQ
     ERLEKQNIDR KNKKEISWGS QIRNYVFQPY TLVKDVRTGY EVGNIQAMMD GELLDAFIKA
     YLVDYGEIT