RF2_BORA1
ID RF2_BORA1 Reviewed; 367 AA.
AC Q2L224;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=BAV1519;
OS Bordetella avium (strain 197N).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N;
RX PubMed=16885469; DOI=10.1128/jb.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ49132.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2L224; -.
DR SMR; Q2L224; -.
DR STRING; 360910.BAV1519; -.
DR EnsemblBacteria; CAJ49132; CAJ49132; BAV1519.
DR KEGG; bav:BAV1519; -.
DR eggNOG; COG1186; Bacteria.
DR HOGENOM; CLU_220733_0_1_4; -.
DR OMA; YVFHPYQ; -.
DR Proteomes; UP000001977; 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_1000004972"
FT MOD_RES 254
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ SEQUENCE 367 AA; 41451 MW; 86C839470F5602CB CRC64;
MEAERQNQIA ARLADYAERE QALRRYLDYD AKTERLHVVN AELEDPAVWN DPKHAQDLGR
EKKSLEDVVQ TLTELGQGVA DALELFELAA ADEDDATLES IENDANTFQE RLEGLEFRRM
FSNPADPLNC FLDIQAGAGG TEAQDWASML LRQYLKYAER KGFKAEVLEE SEGEIAGIKS
ATIKLEGEYA FGYLRTETGV HRLVRKSPFD SSGGRHTSFA SVFVYPEVDE SFEVEVNPAD
LRVDTYRASG AGGQHINKTD SAVRITHMPS GIVVQCQNDR SQHRNRAEAM QMLKSKLYEL
EMRKRMAEQQ KLEDSKTDVG WGHQIRSYVL DQSRIKDLRT NVEISNTQKV LDGDLDPFIQ
ASLKQGV
