ID   RF2_THERP               Reviewed;         374 AA.
AC   B9L0E3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 62.
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=trd_1636;
OS   Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2).
OC   Bacteria; Chloroflexi; Thermomicrobiales; Thermomicrobiaceae;
OC   Thermomicrobium.
OX   NCBI_TaxID=309801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27502 / DSM 5159 / P-2;
RX   PubMed=19148287; DOI=10.1371/journal.pone.0004207;
RA   Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., Bryant D.A.,
RA   Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., Ward N.L.,
RA   Eisen J.A.;
RT   "Complete genome sequence of the aerobic CO-oxidizing thermophile
RT   Thermomicrobium roseum.";
RL   PLoS ONE 4:E4207-E4207(2009).
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; CP001275; ACM04523.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9L0E3; -.
DR   SMR; B9L0E3; -.
DR   STRING; 309801.trd_1636; -.
DR   EnsemblBacteria; ACM04523; ACM04523; trd_1636.
DR   KEGG; tro:trd_1636; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_3423163_0_0_0; -.
DR   OMA; YVFHPYQ; -.
DR   Proteomes; UP000000447; 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..374
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000193560"
FT   MOD_RES         248
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   374 AA;  42359 MW;  5BE767E6D93D85B3 CRC64;
     MAQPMLIDLE ELVERLDRIG VRLCLPSKRQ QIEQLEHEAA DPDLWQDPQR AQSLLRRLSQ
     LRDLVQEWET LSQQARDLLE LRALASDDLE LAGQVEQEAT ELAERVRQLE LRLLLTGQYD
     GHDAILAVHA GTGGVDAQDW AEMLLRMYLR WAQRAGFAAE VVDLLEGEEA GIKSATVEVR
     GPYAYGYLKG EAGTHRLVRL SPFDAAHRRH TSFALVEVLP LVEEDDDVEI REEDIRIDTF
     RASGHGGQHV NKTESAVRIT HLPTGIVVTC QNERSQIQNR ETAMKILKAR LLELKIRQRQ
     EEQARLKGKP VVTGWGNRIR SYVLHPYTMV TDHRTEVSTP NIQAVLEGEI DPFIEAYLHQ
     QAAEGEETAA ASDR