ID   RF2_RICCN               Reviewed;         368 AA.
AC   Q92IQ2;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 103.
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=RC0368;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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; AE006914; AAL02906.1; -; Genomic_DNA.
DR   PIR; H97745; H97745.
DR   AlphaFoldDB; Q92IQ2; -.
DR   SMR; Q92IQ2; -.
DR   KEGG; rco:RC0368; -.
DR   HOGENOM; CLU_221951_1_0_5; -.
DR   Proteomes; UP000000816; 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   Gene3D; 3.30.160.20; -; 1.
DR   Gene3D; 3.30.70.1660; -; 1.
DR   Gene3D; 1.20.58.410; Release factor; 1.
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   NCBIfam; TIGR00020; prfB; 1.
DR   PANTHER; PTHR43116; PEPTIDE CHAIN RELEASE FACTOR 2; 1.
DR   PANTHER; PTHR43116:SF3; RF_PROK_I DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF03462; PCRF; 1.
DR   Pfam; PF00472; RF-1; 1.
DR   SMART; SM00937; PCRF; 1.
DR   SUPFAM; SSF75620; Release factor; 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_0000166838"
FT   MOD_RES         250
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   368 AA;  41540 MW;  A63C0FD338F7081F CRC64;
     MRAEIENYVK KIEQSLELLW RSLDVEASTE RLNALEELTA DPSLWNDQAN AQKLLREKSN
     LEEKLNAFNK LKSNLKDALE LEEMAEAEND LETLSQIEQD LKNLSIIAAK FETECLFSGE
     ADGNNCFLEI NAGAGGTESH DWASIMMRMY LRFAERLGFK TEIINMINGE EAGIKSCTIR
     IIGKRAYGWF KTETGVHRLV RISPFNAAGK RMTSFASSWV YPEIDDNIAI TIEDKDLRID
     TFRASGAGGQ HVNTTDSAVR ITHIPTGTVT QCQSDRSQHK NKAQAMKMLQ AKLYELEMQK
     RTDSVNEQNA AKTDNSWGHQ IRSYVLQPYH MVKDLRTDYE TSDTKGVLDG DLEEFVSAHL
     AMNVGGKK
//