ID RF2_THET8 Reviewed; 378 AA. AC Q5SM01; DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 27-MAR-2024, entry version 117. DE RecName: Full=Peptide chain release factor RF2; GN Name=prfB; OrderedLocusNames=TTHA0142; OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=300852; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27634 / DSM 579 / HB8; RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.; RT "Complete genome sequence of Thermus thermophilus HB8."; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. RN [2] RP INTERACTION WITH E.COLI RIBOSOME, LACK OF FUNCTION IN E.COLI, AND RP METHYLATION AT GLN-253. RX PubMed=28077875; DOI=10.1038/nature21053; RA Zeng F., Chen Y., Remis J., Shekhar M., Phillips J.C., Tajkhorshid E., RA Jin H.; RT "Structural basis of co-translational quality control by ArfA and RF2 bound RT to ribosome."; RL Nature 541:554-557(2017). RN [3] {ECO:0007744|PDB:4V4S} RP X-RAY CRYSTALLOGRAPHY (6.76 ANGSTROMS) OF 28-378 IN COMPLEX WITH 70S RP RIBOSOME, FUNCTION, AND SUBUNIT. RX PubMed=16377566; DOI=10.1016/j.cell.2005.09.039; RA Petry S., Brodersen D.E., Murphy F.V., Dunham C.M., Selmer M., Tarry M.J., RA Kelley A.C., Ramakrishnan V.; RT "Crystal structures of the ribosome in complex with release factors RF1 and RT RF2 bound to a cognate stop codon."; RL Cell 123:1255-1266(2005). RN [4] {ECO:0007744|PDB:2IHR} RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 27-378, AND SUBCELLULAR LOCATION. RX PubMed=17272297; DOI=10.1093/nar/gkl696; RA Zoldak G., Redecke L., Svergun D.I., Konarev P.V., Voertler C.S., RA Dobbek H., Sedlak E., Sprinzl M.; RT "Release factors 2 from Escherichia coli and Thermus thermophilus: RT structural, spectroscopic and microcalorimetric studies."; RL Nucleic Acids Res. 35:1343-1353(2007). RN [5] {ECO:0007744|PDB:4V5E} RP X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS) OF 31-369 IN COMPLEX WITH 70S RP RIBOSOME, INTERACTION WITH L11, INTERACTION WITH 23S RRNA, AND SUBUNIT. RX PubMed=18988853; DOI=10.1126/science.1164840; RA Weixlbaumer A., Jin H., Neubauer C., Voorhees R.M., Petry S., Kelley A.C., RA Ramakrishnan V.; RT "Insights into translational termination from the structure of RF2 bound to RT the ribosome."; RL Science 322:953-956(2008). RN [6] {ECO:0007744|PDB:4V5J} RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 31-369 IN COMPLEX WITH 70S RP RIBOSOME, INTERACTION WITH 23S RRNA, AND SUBUNIT. RX PubMed=20421507; DOI=10.1073/pnas.1003995107; RA Jin H., Kelley A.C., Loakes D., Ramakrishnan V.; RT "Structure of the 70S ribosome bound to release factor 2 and a substrate RT analog provides insights into catalysis of peptide release."; RL Proc. Natl. Acad. Sci. U.S.A. 107:8593-8598(2010). RN [7] {ECO:0007744|PDB:5MDY} RP STRUCTURE BY ELECTRON MICROSCOPY (3.35 ANGSTROMS) IN COMPLEX WITH E.COLI RP 70S RIBOSOME AND E.COLI ARFA, FUNCTION, AND INTERACTION WITH ARFA. RC STRAIN=ATCC 27634 / DSM 579 / HB8; RX PubMed=27934701; DOI=10.1126/science.aai9127; RA James N.R., Brown A., Gordiyenko Y., Ramakrishnan V.; RT "Translational termination without a stop codon."; RL Science 354:1437-1440(2016). 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 (Probable). In endogenous ribosomes interacts with P-site tRNA and CC 23S rRNA (PubMed:18988853, PubMed:20421507). In the presence of CC truncated mRNA in the 70S ribosome, ArfA and RF2 interact such that the CC GGQ peptide hydrolysis motif of RF2 rises into the peptidyl-transferase CC center and releases the ribosome (By similarity). Recruited to stalled CC E.coli 70S ribosomes by E.coli ArfA, but cannot be functionally CC accomodated in the peptidyl-transferase center (PubMed:27934701, CC PubMed:28077875). Note T.thermophilus probably does not encode arfA CC (Ref.1). {ECO:0000250|UniProtKB:P07012, ECO:0000269|PubMed:18988853, CC ECO:0000269|PubMed:20421507, ECO:0000269|PubMed:27934701, CC ECO:0000269|PubMed:28077875, ECO:0000305|PubMed:16377566, CC ECO:0000305|Ref.1}. CC -!- SUBUNIT: Interacts with the ribosome (PubMed:16377566, PubMed:17272297, CC PubMed:18988853, PubMed:20421507). Interacts with ribosomal protein L11 CC (PubMed:18988853). Recruited to stalled E.coli ribosomes by E.coli ArfA CC (PubMed:27934701, PubMed:28077875). {ECO:0000269|PubMed:16377566, CC ECO:0000269|PubMed:17272297, ECO:0000269|PubMed:18988853, CC ECO:0000269|PubMed:20421507, ECO:0000269|PubMed:28077875, CC ECO:0000305|PubMed:27934701}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:17272297}. CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor CC family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP008226; BAD69965.1; -; Genomic_DNA. DR RefSeq; YP_143408.1; NC_006461.1. DR PDB; 2IHR; X-ray; 2.50 A; 1=27-378. DR PDB; 4V4S; X-ray; 6.76 A; AY=28-378. DR PDB; 4V5E; X-ray; 3.45 A; AY/CY=31-369. DR PDB; 4V5J; X-ray; 3.10 A; AY/CY=31-369. DR PDB; 4V67; X-ray; 3.00 A; AX/CX=1-378. DR PDB; 5MDY; EM; 3.35 A; 7=1-378. DR PDB; 6C5L; X-ray; 3.20 A; AY/CY=28-369. DR PDBsum; 2IHR; -. DR PDBsum; 4V4S; -. DR PDBsum; 4V5E; -. DR PDBsum; 4V5J; -. DR PDBsum; 4V67; -. DR PDBsum; 5MDY; -. DR PDBsum; 6C5L; -. DR AlphaFoldDB; Q5SM01; -. DR EMDB; EMD-3492; -. DR SMR; Q5SM01; -. DR IntAct; Q5SM01; 51. DR iPTMnet; Q5SM01; -. DR EnsemblBacteria; BAD69965; BAD69965; BAD69965. DR KEGG; ttj:TTHA0142; -. DR PATRIC; fig|300852.9.peg.140; -. DR eggNOG; COG1186; Bacteria. DR HOGENOM; CLU_036856_6_0_0; -. DR PhylomeDB; Q5SM01; -. DR EvolutionaryTrace; Q5SM01; -. DR Proteomes; UP000000532; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR Gene3D; 3.30.160.20; -; 1. DR Gene3D; 3.30.70.1660; -; 1. DR Gene3D; 1.20.58.410; Release factor; 1. 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 NCBIfam; TIGR00020; prfB; 1. DR PANTHER; PTHR43116; PEPTIDE CHAIN RELEASE FACTOR 2; 1. DR PANTHER; PTHR43116:SF3; RF_PROK_I DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF03462; PCRF; 1. DR Pfam; PF00472; RF-1; 1. DR SMART; SM00937; PCRF; 1. DR SUPFAM; SSF75620; Release factor; 1. DR PROSITE; PS00745; RF_PROK_I; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Methylation; Protein biosynthesis; KW Reference proteome; RNA-binding; rRNA-binding; tRNA-binding. FT CHAIN 1..378 FT /note="Peptide chain release factor RF2" FT /id="PRO_0000439755" FT MOD_RES 253 FT /note="N5-methylglutamine" FT /evidence="ECO:0000305|PubMed:28077875" FT STRAND 29..31 FT /evidence="ECO:0007829|PDB:2IHR" FT HELIX 32..39 FT /evidence="ECO:0007829|PDB:2IHR" FT TURN 40..44 FT /evidence="ECO:0007829|PDB:2IHR" FT HELIX 49..51 FT /evidence="ECO:0007829|PDB:2IHR" FT TURN 52..54 FT /evidence="ECO:0007829|PDB:2IHR" FT HELIX 55..57 FT /evidence="ECO:0007829|PDB:2IHR" FT STRAND 58..60 FT /evidence="ECO:0007829|PDB:2IHR" FT HELIX 63..67 FT /evidence="ECO:0007829|PDB:2IHR" FT HELIX 69..81 FT /evidence="ECO:0007829|PDB:2IHR" FT TURN 82..84 FT /evidence="ECO:0007829|PDB:2IHR" FT HELIX 85..88 FT /evidence="ECO:0007829|PDB:2IHR" FT HELIX 97..99 FT /evidence="ECO:0007829|PDB:2IHR" FT HELIX 101..103 FT /evidence="ECO:0007829|PDB:2IHR" FT HELIX 105..119 FT /evidence="ECO:0007829|PDB:2IHR" FT STRAND 122..124 FT /evidence="ECO:0007829|PDB:2IHR" FT STRAND 127..135 FT /evidence="ECO:0007829|PDB:2IHR" FT HELIX 140..158 FT /evidence="ECO:0007829|PDB:2IHR" FT TURN 159..161 FT /evidence="ECO:0007829|PDB:2IHR" FT STRAND 163..171 FT /evidence="ECO:0007829|PDB:2IHR" FT STRAND 173..186 FT /evidence="ECO:0007829|PDB:2IHR" FT HELIX 189..193 FT /evidence="ECO:0007829|PDB:2IHR" FT HELIX 194..196 FT /evidence="ECO:0007829|PDB:2IHR" FT STRAND 198..205 FT /evidence="ECO:0007829|PDB:2IHR" FT STRAND 209..211 FT /evidence="ECO:0007829|PDB:2IHR" FT STRAND 214..226 FT /evidence="ECO:0007829|PDB:2IHR" FT STRAND 229..232 FT /evidence="ECO:0007829|PDB:2IHR" FT HELIX 237..239 FT /evidence="ECO:0007829|PDB:2IHR" FT STRAND 240..245 FT /evidence="ECO:0007829|PDB:2IHR" FT HELIX 255..257 FT /evidence="ECO:0007829|PDB:2IHR" FT STRAND 260..266 FT /evidence="ECO:0007829|PDB:2IHR" FT TURN 267..269 FT /evidence="ECO:0007829|PDB:2IHR" FT STRAND 272..275 FT /evidence="ECO:0007829|PDB:2IHR" FT STRAND 277..279 FT /evidence="ECO:0007829|PDB:2IHR" FT HELIX 281..307 FT /evidence="ECO:0007829|PDB:2IHR" FT TURN 308..312 FT /evidence="ECO:0007829|PDB:2IHR" FT STRAND 324..328 FT /evidence="ECO:0007829|PDB:2IHR" FT HELIX 329..331 FT /evidence="ECO:0007829|PDB:2IHR" FT STRAND 333..336 FT /evidence="ECO:0007829|PDB:2IHR" FT TURN 337..339 FT /evidence="ECO:0007829|PDB:2IHR" FT STRAND 342..344 FT /evidence="ECO:0007829|PDB:2IHR" FT HELIX 346..349 FT /evidence="ECO:0007829|PDB:2IHR" FT TURN 350..352 FT /evidence="ECO:0007829|PDB:2IHR" FT HELIX 355..366 FT /evidence="ECO:0007829|PDB:2IHR" SQ SEQUENCE 378 AA; 42734 MW; 55B4AC9C891AEEB7 CRC64; MRLASQSAIL VKVWTWNASR NAWKASGGIF DIPQKETRLK ELERRLEDPS LWNDPEAARK VSQEAARLRR TVDTFRSLES DLQGLLELME ELPAEEREAL KPELEEAAKK LDELYHQTLL NFPHAEKNAI LTIQPGAGGT EACDWAEMLL RMYTRFAERQ GFQVEVVDLT PGPEAGIDYA QILVKGENAY GLLSPEAGVH RLVRPSPFDA SGRRHTSFAG VEVIPEVDEE VEVVLKPEEL RIDVMRASGP GGQGVNTTDS AVRVVHLPTG ITVTCQTTRS QIKNKELALK ILKARLYELE RKKREEELKA LRGEVRPIEW GSQIRSYVLD KNYVKDHRTG LMRHDPENVL DGDLMDLIWA GLEWKAGRRQ GTEEVEAE //