ID   RF2_PETMO               Reviewed;         366 AA.
AC   A9BHH8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=Pmob_0864;
OS   Petrotoga mobilis (strain DSM 10674 / SJ95).
OC   Bacteria; Thermotogae; Petrotogales; Petrotogaceae; Petrotoga.
OX   NCBI_TaxID=403833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10674 / SJ95;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Noll K., Richardson P.;
RT   "Complete sequence of Petroga mobilis SJ95.";
RL   Submitted (NOV-2007) 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; CP000879; ABX31587.1; -; Genomic_DNA.
DR   RefSeq; WP_012208690.1; NC_010003.1.
DR   AlphaFoldDB; A9BHH8; -.
DR   SMR; A9BHH8; -.
DR   STRING; 403833.Pmob_0864; -.
DR   PRIDE; A9BHH8; -.
DR   EnsemblBacteria; ABX31587; ABX31587; Pmob_0864.
DR   KEGG; pmo:Pmob_0864; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_036856_6_0_0; -.
DR   OMA; YVFHPYQ; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000000789; 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..366
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000075527"
FT   MOD_RES         249
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   366 AA;  42227 MW;  EC8168B064D9CFE9 CRC64;
     MIEYETKVKI DELKENFEDL KDVFNIDKVE EEVKKLDKEM MEPNFWNDQN RAKKISKMAQ
     NLKDEIDEFK KLENDFEELE IAVELSEDDP SMTAQVEAIL KVIEKKIGSF RLRMLLSEEY
     DDANAFLSLH PGAGGTESQD WASMLLRMYT RWADKNNYDI ETIDFQEGDE AGIKSATIKI
     SGPYAYGKLK YESGVHRLVR ISPFDANGRR HTSFASISVM PEFDENVEIE INPDDLKIDT
     YRSGGAGGQH VNKTDSAVRI THLPTGIVVA VQNERSQHQN KATALKILKA KLYELEHQKK
     LEEKLRLRGE VKDISWGNQI RSYVLYPYTL VKDLRTEYET SNAQAVLDGE IDEFIEEELL
     FFAKYK