ID   RF2_ACIF2               Reviewed;         365 AA.
AC   B7J4M2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 61.
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=AFE_0479;
OS   Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768
OS   / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)).
OC   Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=243159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455;
RX   PubMed=19077236; DOI=10.1186/1471-2164-9-597;
RA   Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R. II,
RA   Eisen J.A., Holmes D.S.;
RT   "Acidithiobacillus ferrooxidans metabolism: from genome sequence to
RT   industrial applications.";
RL   BMC Genomics 9:597-597(2008).
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; CP001219; ACK79718.1; -; Genomic_DNA.
DR   AlphaFoldDB; B7J4M2; -.
DR   SMR; B7J4M2; -.
DR   STRING; 243159.AFE_0479; -.
DR   PaxDb; B7J4M2; -.
DR   EnsemblBacteria; ACK79718; ACK79718; AFE_0479.
DR   KEGG; afr:AFE_0479; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_3418673_0_0_6; -.
DR   OMA; YVFHPYQ; -.
DR   Proteomes; UP000001362; 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.
FT   CHAIN           1..365
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000117256"
FT   MOD_RES         252
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   365 AA;  40567 MW;  F3CE4FA4A5830594 CRC64;
     MREVNEMRAL HDDLQVRVAG LRGYLDLEEK RGRLEEVQRE LEDPTIWNNA EKAQELGRER
     SALEAVITPM DKLTASLADG GEMLELALSE QDAELLAAVD ADLDTALSLV EKLEFQRMFS
     GAQDAANCFV DIQAGAGGTE AQDWAEMILR MYLHWAESHG FAAELVEVSE GEVAGIKSAS
     IHVRGDHAFG WLRTETGVHR LVRKSPFDSG NRRHTSFASV FVYPEIDDSF EVDINPADLK
     VDTYRASGAG GQHVNKTDSA IRITHVPSGI VVACQTDRSQ HKNRAEAMRM LRSKLYEMEM
     QKRAVEKQAL EDSKSDIGWG HQIRSYVLDQ SRIKDLRTGV EVGDTQKVLD GALDMFIEAA
     LKAGL