ID   RF2_SALTO               Reviewed;         373 AA.
AC   A4X3K6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=Strop_0981;
OS   Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Salinispora.
OX   NCBI_TaxID=369723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440;
RX   PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA   Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA   Jensen P.R., Moore B.S.;
RT   "Genome sequencing reveals complex secondary metabolome in the marine
RT   actinomycete Salinispora tropica.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
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; CP000667; ABP53456.1; -; Genomic_DNA.
DR   RefSeq; WP_011904890.1; NC_009380.1.
DR   AlphaFoldDB; A4X3K6; -.
DR   SMR; A4X3K6; -.
DR   STRING; 369723.Strop_0981; -.
DR   EnsemblBacteria; ABP53456; ABP53456; Strop_0981.
DR   KEGG; stp:Strop_0981; -.
DR   PATRIC; fig|369723.5.peg.1000; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_036856_6_0_11; -.
DR   OMA; YVFHPYQ; -.
DR   Proteomes; UP000000235; 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..373
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000075529"
FT   MOD_RES         251
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   373 AA;  41382 MW;  36C4FAF44C7A3FA7 CRC64;
     MTDADYAEQL KDLDATLRNI ESVLDIDRLR ADKARLEEAA SAPDLWDDQA RAQQVTSQLS
     YVNGEINKLA ELRSRLDDAK VLLELAEAES DPGALTEVEA EVAGLAKAID EMEVRTLLSG
     EYDSREALVA IRAGAGGVDA ADFAEMLLRM YLRWAERHGY PTEVYETSYA EEAGLKSATF
     TVKVPYAYGT LSVESGTHRL VRISPFDNQG RRQTSFAGVE VLPVVEQTDH IDIPENEMRF
     DVYRSSGPGG QSVNTTDSAV RITHIPTGIV VTCQNEKSQL QNKASALRVL QARLLERKRQ
     EEQAKLQGLK TDAAGSWGDQ MRSYVLHPYQ MVKDLRTEQE TGTPAAVFDG ELDAFIEAGI
     RWRKQQQLAD DNA