ID SSRP_THET8 Reviewed; 144 AA. AC Q8RR57; Q5SMG1; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 27-MAR-2024, entry version 116. DE RecName: Full=SsrA-binding protein {ECO:0000255|HAMAP-Rule:MF_00023}; DE AltName: Full=Small protein B {ECO:0000255|HAMAP-Rule:MF_00023}; GN Name=smpB {ECO:0000255|HAMAP-Rule:MF_00023}; GN OrderedLocusNames=TTHA0902; 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 [GENOMIC DNA]. RA Nameki N., Kimoto M., Terada T., Shirouzu M., Suetsugu-Hanawa K., RA Takaku H., Himeno H., Muto A., Inoue Y., Shibata T., Kuramitsu S., RA Yokoyama S., Kawai G.; RT "Interaction of tmRNA with a tmRNA-binding protein, SmpB, from Thermus RT thermophilus."; RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases. RN [2] 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 [3] RP STRUCTURE BY NMR. RC STRAIN=ATCC 27634 / DSM 579 / HB8; RX PubMed=12560085; DOI=10.1016/s0014-5793(02)03880-2; RA Someya T., Nameki N., Hosoi H., Suzuki S., Hatanaka H., Fujii M., RA Terada T., Shirouzu M., Inoue Y., Shibata T., Kuramitsu S., Yokoyama S., RA Kawai G.; RT "Solution structure of a tmRNA-binding protein, SmpB, from Thermus RT thermophilus."; RL FEBS Lett. 535:94-100(2003). RN [4] RP STRUCTURE BY ELECTRON MICROSCOPY (13.00 ANGSTROMS), FUNCTION, SUBUNIT, RP RRNA-BINDING, AND TMRNA-BINDING. RX PubMed=12677067; DOI=10.1126/science.1081798; RA Valle M., Gillet R., Kaur S., Henne A., Ramakrishnan V., Frank J.; RT "Visualizing tmRNA entry into a stalled ribosome."; RL Science 300:127-130(2003). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-123 IN COMPLEX WITH TMRNA, RP FUNCTION, SUBUNIT, AND TMRNA-BINDING. RX PubMed=17488812; DOI=10.1073/pnas.0700402104; RA Bessho Y., Shibata R., Sekine S., Murayama K., Higashijima K., RA Hori-Takemoto C., Shirouzu M., Kuramitsu S., Yokoyama S.; RT "Structural basis for functional mimicry of long-variable-arm tRNA by RT transfer-messenger RNA."; RL Proc. Natl. Acad. Sci. U.S.A. 104:8293-8298(2007). RN [6] RP STRUCTURE BY ELECTRON MICROSCOPY (13.00 ANGSTROMS) OF 2-144 IN COMPLEX WITH RP TMRNA AND 70S RIBOSOMES, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, RP TMRNA-BINDING, AND RRNA-BINDING. RC STRAIN=ATCC 27634 / DSM 579 / HB8; RX PubMed=20953161; DOI=10.1038/emboj.2010.252; RA Weis F., Bron P., Giudice E., Rolland J.P., Thomas D., Felden B., RA Gillet R.; RT "tmRNA-SmpB: a journey to the centre of the bacterial ribosome."; RL EMBO J. 29:3810-3818(2010). RN [7] RP STRUCTURE BY ELECTRON MICROSCOPY (13.60 ANGSTROMS) OF 2-123 IN COMPLEX WITH RP TMRNA AND 70S RIBOSOMES, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=20940705; DOI=10.1038/emboj.2010.255; RA Fu J., Hashem Y., Wower I., Lei J., Liao H.Y., Zwieb C., Wower J., RA Frank J.; RT "Visualizing the transfer-messenger RNA as the ribosome resumes RT translation."; RL EMBO J. 29:3819-3825(2010). RN [8] RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) IN COMPLEX WITH TMRNA AND 70S RP RIBOSOMES, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, RRNA-BINDING, AND RP TNRNA-BINDING. RC STRAIN=ATCC 27634 / DSM 579 / HB8; RX PubMed=22422985; DOI=10.1126/science.1217039; RA Neubauer C., Gillet R., Kelley A.C., Ramakrishnan V.; RT "Decoding in the absence of a codon by tmRNA and SmpB in the ribosome."; RL Science 335:1366-1369(2012). RN [9] RP STRUCTURE BY ELECTRON MICROSCOPY (8.30 ANGSTROMS) OF 1-123 IN COMPLEX WITH RP TMRNA AND 70S RIBOSOMES, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=22622583; DOI=10.1038/nature11006; RA Ramrath D.J., Yamamoto H., Rother K., Wittek D., Pech M., Mielke T., RA Loerke J., Scheerer P., Ivanov P., Teraoka Y., Shpanchenko O., RA Nierhaus K.H., Spahn C.M.; RT "The complex of tmRNA-SmpB and EF-G on translocating ribosomes."; RL Nature 485:526-529(2012). CC -!- FUNCTION: Required for rescue of stalled ribosomes mediated by trans- CC translation. Binds to tmRNA (also known as SsrA and 10Sa), required for CC stable association of tmRNA with ribosomes, probably by bridging tmRNA CC to 50S subunit. tmRNA and SmpB together mimic tRNA shape, replacing the CC anticodon stem-loop with SmpB (PubMed:22422985, PubMed:17488812). tmRNA CC is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) CC and it encodes a 'tag peptide', a short internal open reading frame. CC During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, CC entering the A-site of stalled ribosomes, displacing the stalled mRNA. CC The ribosome then switches to translate the ORF on the tmRNA; the CC nascent peptide is terminated with the 'tag peptide' encoded by the CC tmRNA and targeted for degradation. The ribosome is freed to recommence CC translation, which seems to be the essential function of trans- CC translation. {ECO:0000255|HAMAP-Rule:MF_00023, CC ECO:0000269|PubMed:12677067, ECO:0000269|PubMed:17488812, CC ECO:0000269|PubMed:20940705, ECO:0000269|PubMed:20953161, CC ECO:0000269|PubMed:22422985, ECO:0000269|PubMed:22622583}. CC -!- SUBUNIT: Binds tmRNA (PubMed:12677067, PubMed:20953161, CC PubMed:22422985, PubMed:17488812, PubMed:20940705, PubMed:22622583). CC Binds to both the 50S and 30S ribosomal subunits via rRNA contacts, CC bridges tmRNA binding to stalled ribosomes. CC {ECO:0000269|PubMed:12677067, ECO:0000269|PubMed:17488812, CC ECO:0000269|PubMed:20940705, ECO:0000269|PubMed:20953161, CC ECO:0000269|PubMed:22422985, ECO:0000269|PubMed:22622583}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00023}. CC Note=The tmRNA-SmpB complex associates with stalled 70S ribosomes CC (PubMed:20953161, PubMed:22422985, PubMed:20940705, PubMed:22622583). CC {ECO:0000255|HAMAP-Rule:MF_00023, ECO:0000269|PubMed:20940705, CC ECO:0000269|PubMed:20953161, ECO:0000269|PubMed:22422985, CC ECO:0000269|PubMed:22622583}. CC -!- MISCELLANEOUS: Athough the Valle et al., electron microscopy paper CC indicates this protein came from T.thermophilus, its sequence maps to CC A.aeolicus (PubMed:12677067). The Fu et al., paper maps the coordinates CC of T.thermophilus to E.coli (PubMed:20940705). CC {ECO:0000305|PubMed:12677067, ECO:0000305|PubMed:20940705}. CC -!- SIMILARITY: Belongs to the SmpB family. {ECO:0000255|HAMAP- CC Rule:MF_00023}. 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; AB070601; BAB86918.1; -; Genomic_DNA. DR EMBL; AP008226; BAD70725.1; -; Genomic_DNA. DR RefSeq; WP_011172991.1; NC_006461.1. DR RefSeq; YP_144168.1; NC_006461.1. DR PDB; 1J1H; NMR; -; A=1-144. DR PDB; 1WJX; X-ray; 1.70 A; A=2-123. DR PDB; 2CZJ; X-ray; 3.01 A; A/C/E/G=1-123. DR PDB; 3IYQ; EM; -; B=2-144. DR PDB; 3IYR; EM; -; B=2-144. DR PDB; 3IZ4; EM; -; B=2-123. DR PDB; 4V6T; EM; 8.30 A; W=1-123. DR PDB; 4V8Q; X-ray; 3.10 A; B2=1-144. DR PDB; 6Q95; EM; 3.70 A; 5=1-144. DR PDBsum; 1J1H; -. DR PDBsum; 1WJX; -. DR PDBsum; 2CZJ; -. DR PDBsum; 3IYQ; -. DR PDBsum; 3IYR; -. DR PDBsum; 3IZ4; -. DR PDBsum; 4V6T; -. DR PDBsum; 4V8Q; -. DR PDBsum; 6Q95; -. DR AlphaFoldDB; Q8RR57; -. DR EMDB; EMD-4475; -. DR SMR; Q8RR57; -. DR EnsemblBacteria; BAD70725; BAD70725; BAD70725. DR GeneID; 3169917; -. DR KEGG; ttj:TTHA0902; -. DR PATRIC; fig|300852.9.peg.894; -. DR eggNOG; COG0691; Bacteria. DR HOGENOM; CLU_108953_0_0_0; -. DR PhylomeDB; Q8RR57; -. DR EvolutionaryTrace; Q8RR57; -. 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:0070929; P:trans-translation; IEA:UniProtKB-UniRule. DR CDD; cd09294; SmpB; 1. DR Gene3D; 2.40.280.10; -; 1. DR HAMAP; MF_00023; SmpB; 1. DR InterPro; IPR023620; SmpB. DR InterPro; IPR000037; SsrA-bd_prot. DR InterPro; IPR020081; SsrA-bd_prot_CS. DR NCBIfam; TIGR00086; smpB; 1. DR PANTHER; PTHR30308:SF2; SSRA-BINDING PROTEIN; 1. DR PANTHER; PTHR30308; TMRNA-BINDING COMPONENT OF TRANS-TRANSLATION TAGGING COMPLEX; 1. DR Pfam; PF01668; SmpB; 1. DR SUPFAM; SSF74982; Small protein B (SmpB); 1. DR PROSITE; PS01317; SSRP; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Reference proteome; RNA-binding; rRNA-binding. FT CHAIN 1..144 FT /note="SsrA-binding protein" FT /id="PRO_0000103056" FT HELIX 8..13 FT /evidence="ECO:0007829|PDB:1WJX" FT STRAND 14..24 FT /evidence="ECO:0007829|PDB:1WJX" FT HELIX 30..35 FT /evidence="ECO:0007829|PDB:1WJX" FT STRAND 45..49 FT /evidence="ECO:0007829|PDB:1WJX" FT STRAND 52..57 FT /evidence="ECO:0007829|PDB:1WJX" FT STRAND 60..63 FT /evidence="ECO:0007829|PDB:1J1H" FT STRAND 77..80 FT /evidence="ECO:0007829|PDB:1WJX" FT HELIX 83..89 FT /evidence="ECO:0007829|PDB:1WJX" FT TURN 90..92 FT /evidence="ECO:0007829|PDB:1WJX" FT TURN 94..97 FT /evidence="ECO:0007829|PDB:1J1H" FT STRAND 98..107 FT /evidence="ECO:0007829|PDB:1WJX" FT TURN 109..111 FT /evidence="ECO:0007829|PDB:1J1H" FT STRAND 113..122 FT /evidence="ECO:0007829|PDB:1WJX" SQ SEQUENCE 144 AA; 16750 MW; 4691B4D48F1A2299 CRC64; MAPVLENRRA RHDYEILETY EAGIALKGTE VKSLRAGKVD FTGSFARFED GELYLENLYI APYEKGSYAN VDPRRKRKLL LHKHELRRLL GKVEQKGLTL VPLKIYFNER GYAKVLLGLA RGKKAYEKRR EDKKEAVRRA LEEL //