ID   RF2_RICPR               Reviewed;         369 AA.
AC   Q9ZDQ2;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Peptide chain release factor 2;
DE            Short=RF-2;
GN   Name=prfB; OrderedLocusNames=RP274;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ235271; CAA14736.1; -; Genomic_DNA.
DR   PIR; F71682; F71682.
DR   RefSeq; NP_220659.2; NC_000963.1.
DR   AlphaFoldDB; Q9ZDQ2; -.
DR   SMR; Q9ZDQ2; -.
DR   STRING; 272947.RP274; -.
DR   EnsemblBacteria; CAA14736; CAA14736; CAA14736.
DR   KEGG; rpr:RP274; -.
DR   PATRIC; fig|272947.5.peg.281; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_221951_1_0_5; -.
DR   OMA; YVFHPYQ; -.
DR   Proteomes; UP000002480; 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_0000166840"
FT   MOD_RES         250
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   369 AA;  42095 MW;  0DADDD8DA4632823 CRC64;
     MRAEIENYIK KIEQSLDLIW RSLDIEALTV RLTELEELTA DPNLWNNNAN AQTLLREKNN
     LEEKLNVFNK LKSNLKEILE LEAMAEVEND LETLNQIEQD FKKLSIITAK FETECLFSGE
     TDCNNCFLEI NAGAGGTESH DWASIMMRMY LRFAERLGFK TKIINMINGE EVGIKSCTIR
     IIGKRAYGWF KTESGVHRLV RISPFNAAGK RMTSFASSWI YPEIDDDIAI TIEDKDLRID
     TFRSSGAGGQ HVNTTDSAVR ITHIPTNTVT QCQSDRSQHK NKAQAMKMLQ AKLYKLEMQK
     RNENVDKQNA NKTDNSWGHQ IRSYVLQPYQ IVKDLRTNYE TSDTKGVLDG NLEDFVSASL
     SMNNSGNKT