RF2_RICAE
ID RF2_RICAE Reviewed; 368 AA.
AC C3PMX2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 25-MAY-2022, entry version 65.
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=RAF_ORF0343;
OS Rickettsia africae (strain ESF-5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=347255;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ESF-5;
RX PubMed=19379498; DOI=10.1186/1471-2164-10-166;
RA Fournier P.-E., El Karkouri K., Leroy Q., Robert C., Giumelli B.,
RA Renesto P., Socolovschi C., Parola P., Audic S., Raoult D.;
RT "Analysis of the Rickettsia africae genome reveals that virulence
RT acquisition in Rickettsia species may be explained by genome reduction.";
RL BMC Genomics 10:166-166(2009).
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; CP001612; ACP53282.1; -; Genomic_DNA.
DR RefSeq; WP_012719532.1; NC_012633.1.
DR AlphaFoldDB; C3PMX2; -.
DR SMR; C3PMX2; -.
DR EnsemblBacteria; ACP53282; ACP53282; RAF_ORF0343.
DR KEGG; raf:RAF_ORF0343; -.
DR HOGENOM; CLU_036856_6_0_5; -.
DR OMA; YVFHPYQ; -.
DR Proteomes; UP000002305; 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_1000202714"
FT MOD_RES 250
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ SEQUENCE 368 AA; 41577 MW; 46285E70F74A6905 CRC64;
MRTEIENYVK 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 TKTDNSWGHQ IRSYVLQPYH MVKDLRTDYE TSDTKGVLDG DLEEFVSANL
AMNVGGKK