ID   RF2_HAEDU               Reviewed;         365 AA.
AC   Q7VNG1;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   03-AUG-2022, entry version 95.
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=HD_0575;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
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-25; 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; AE017143; AAP95510.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q7VNG1; -.
DR   SMR; Q7VNG1; -.
DR   STRING; 233412.HD_0575; -.
DR   PRIDE; Q7VNG1; -.
DR   EnsemblBacteria; AAP95510; AAP95510; HD_0575.
DR   KEGG; hdu:HD_0575; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_036856_6_0_6; -.
DR   Proteomes; UP000001022; 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..365
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_0000166819"
FT   MOD_RES         252
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   365 AA;  41354 MW;  A729DFF5B829F994 CRC64;
     MFELNPIRTQ LADLTERTQL IRGYLDFDTK VERLEEVNAE LEQPEIWNTP EKAQTLGKER
     STLEMVVNTI NALIQGIEDV EALIELAVEA EDEQTLYEAQ IEADELATKL AKLEFQRMFS
     GPYDATDCYL DLQAGSGGTE AQDWTEMLLR MYLRWAESKG FKTELIEVSD GDVAGLKSAT
     IRITGEYAFG WLRTETGIHR LVRKSPFDSN NRRHTSFAAA FVYPEVDDDV DIEINPADLR
     IDVYRASGAG GQHVNKTESA VRITHMPSGI VVQCQNGRSQ HQNKDQCMKQ LRAKLYEMEM
     MKKNAEKQAM EENKSDIGWG SQIRSYVLDD SRIKDLRTGV ENRNTQAVLD GDLDRFIEAS
     LKAGL