ID   RF2_ACIET               Reviewed;         367 AA.
AC   B9MBK7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-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=Dtpsy_2248;
OS   Acidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Diaphorobacter.
OX   NCBI_TaxID=535289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TPSY;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Coates J.D.;
RT   "Complete sequence of Diaphorobacter sp. TPSY.";
RL   Submitted (JAN-2009) 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   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000255|HAMAP-Rule:MF_00094}.
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DR   EMBL; CP001392; ACM33686.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9MBK7; -.
DR   SMR; B9MBK7; -.
DR   STRING; 535289.Dtpsy_2248; -.
DR   EnsemblBacteria; ACM33686; ACM33686; Dtpsy_2248.
DR   KEGG; dia:Dtpsy_2248; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_220733_0_1_4; -.
DR   OMA; YVFHPYQ; -.
DR   Proteomes; UP000000450; 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..367
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000193551"
FT   MOD_RES         254
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   367 AA;  41518 MW;  3754EECB8AEBD8B5 CRC64;
     MEAERINLIG TTLEDLTERT QELRRYLDYD AKFERLRTVN ASLEDPAVWN DPKKAQELGK
     EKKSLDAVVL TLQKLTTELA DNAELYEMSK EEGDEAGLTT IEAEAEKLRP LIEELEFRRM
     FSNEADPLNC FVDIQAGAGG TEACDWASML LRQYLKYAER KGFKATVEEE TPGDVAGIKS
     ATIKIEGEYA YGLLRTETGV HRLVRKSPFD SSGGRHTSFA SLFVYPEIDD SIEININPSD
     VRTDTYRASG AGGQHINKTD SAVRLTHIPT GIVVQCQDGR SQHSNRDVAW QRLRSRLYDF
     EMRKRMEEQQ KLEDTKTDVG WGHQIRSYVL DNSRIKDLRT NVEVSATQKV LDGDLDVFIE
     ASLKQGV