RF2_THET8
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 25-MAY-2022, entry version 111.
DE RecName: Full=Peptide chain release factor RF2;
GN Name=prfB; OrderedLocusNames=TTHA0142;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; 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.
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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; 5MDY; EM; 3.35 A; 7=1-378.
DR PDBsum; 2IHR; -.
DR PDBsum; 4V4S; -.
DR PDBsum; 4V5E; -.
DR PDBsum; 4V5J; -.
DR PDBsum; 5MDY; -.
DR AlphaFoldDB; Q5SM01; -.
DR SMR; Q5SM01; -.
DR IntAct; Q5SM01; 51.
DR STRING; 300852.55771524; -.
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 OMA; YVFHPYQ; -.
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 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 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
