RF2_BORPE
ID RF2_BORPE Reviewed; 367 AA.
AC Q7VZ35;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 94.
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=BP1104;
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
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 -!- MISCELLANEOUS: The gene for this protein contains a UGA in-frame
CC termination codon after Leu-27; 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:0000255|HAMAP-Rule:MF_00094}.
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DR EMBL; BX640414; CAE41402.1; -; Genomic_DNA.
DR RefSeq; NP_879885.1; NC_002929.2.
DR RefSeq; WP_010926448.1; NZ_CP039022.1.
DR AlphaFoldDB; Q7VZ35; -.
DR SMR; Q7VZ35; -.
DR STRING; 257313.BP1104; -.
DR GeneID; 56478410; -.
DR KEGG; bpe:BP1104; -.
DR PATRIC; fig|257313.5.peg.1182; -.
DR eggNOG; COG1186; Bacteria.
DR HOGENOM; CLU_220733_0_1_4; -.
DR OMA; YVFHPYQ; -.
DR Proteomes; UP000002676; 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..367
FT /note="Peptide chain release factor 2"
FT /id="PRO_1000004975"
FT MOD_RES 254
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ SEQUENCE 367 AA; 41465 MW; 4B965BC8DC242502 CRC64;
MEAERQNQLV ARLEDYAERE QALRRYLDYD AKSERLQVVN AELEDPAIWN DPKHAQDLGR
EKKSLEDVVE TLTELGSGLA DSCELVELAL ADSDDATLEA IEHDADRFQE KLETLEFRRM
FANPADPLNC FVDIQAGAGG TEAQDWASML LRQYLKYAER KGFKAEILEE SEGDVAGLKS
ATIKIEGEYA FGYLRTETGV HRLVRKSPFD SSGGRHTSFA SVFVYPEVDE SFEVEVNPAD
LRIDTYRASG AGGQHINKTD SAVRITHAPS GIVVQCQNDR SQHRNRAEAM QMLKSKLYEL
EMRNRMTEQQ KLEDSKTDVG WGHQIRSYVL DQSRIKDLRT NVEISNTQKV LDGDLDPFIQ
ASLKQGV