ID   RF2_RICFE               Reviewed;         368 AA.
AC   Q4UKS1;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=RF_1001;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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; CP000053; AAY61852.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4UKS1; -.
DR   SMR; Q4UKS1; -.
DR   STRING; 315456.RF_1001; -.
DR   EnsemblBacteria; AAY61852; AAY61852; RF_1001.
DR   KEGG; rfe:RF_1001; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_221951_1_0_5; -.
DR   OMA; YVFHPYQ; -.
DR   Proteomes; UP000008548; 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.
FT   CHAIN           1..368
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_0000166839"
FT   MOD_RES         250
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   368 AA;  41629 MW;  335154D7B1BF0492 CRC64;
     MRAEIENYVK KIEQSLELLW RSLDVESSTE RLNELEELTS DPSLWNDQAN AQTLLREKSN
     LEEKLNAFNK LKSNLKDTLE LEEMAEAEND LETLSQIEQD LKNLSVIAAK FETECLFSGE
     ADGNNCFLEI NAGAGGTESH DWVSIMMRMY LRFAERLGFK TEIINMINGE EAGIKSCTIR
     IIGKRAYGWF KTEAGVHRLV RISPFNAAGK RMTSFASSWV YPEIDDNIAI TIEDKDLRID
     TFRASGAGGQ HVNTTDSAVR ITHIPTNTVT QCQSDRSQHK NKAQAMKMLQ AKLYELEMQK
     RTDSVNEQNA AKTDNSWGHQ IRSYVLQPYQ MVKDLRTDYE TSDTKGVLDG DLEDFVSASL
     AMNAGGRR