ID SSRP_BUCAP Reviewed; 163 AA. AC Q8K9R5; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 109. 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=BUsg_245; OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=198804; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sg; RX PubMed=12089438; DOI=10.1126/science.1071278; RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.; RT "50 million years of genomic stasis in endosymbiotic bacteria."; RL Science 296:2376-2379(2002). CC -!- FUNCTION: Required for rescue of stalled ribosomes mediated by trans- CC translation. Binds to transfer-messenger RNA (tmRNA), required for CC stable association of tmRNA with ribosomes. tmRNA and SmpB together CC mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is CC encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and CC it encodes a 'tag peptide', a short internal open reading frame. During CC trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering CC the A-site of stalled ribosomes, displacing the stalled mRNA. The CC ribosome then switches to translate the ORF on the tmRNA; the nascent CC peptide is terminated with the 'tag peptide' encoded by the tmRNA and CC 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00023}. CC Note=The tmRNA-SmpB complex associates with stalled 70S ribosomes. CC {ECO:0000255|HAMAP-Rule:MF_00023}. 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; AE013218; AAM67804.1; -; Genomic_DNA. DR RefSeq; WP_011053771.1; NC_004061.1. DR AlphaFoldDB; Q8K9R5; -. DR SMR; Q8K9R5; -. DR STRING; 198804.BUsg_245; -. DR GeneID; 75258876; -. DR KEGG; bas:BUsg_245; -. DR eggNOG; COG0691; Bacteria. DR HOGENOM; CLU_108953_3_0_6; -. DR Proteomes; UP000000416; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule. 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 3: Inferred from homology; KW Cytoplasm; RNA-binding. FT CHAIN 1..163 FT /note="SsrA-binding protein" FT /id="PRO_0000102921" SQ SEQUENCE 163 AA; 19246 MW; 637702F33DF7BA08 CRC64; MSYKKKRCLK SSIICKNKKA YYNYFIEEVF QSGLVLMGWE VKSIRLGQVN IIESYINNDN LNEMYLYNSI VQPLHTSSNY VSCDSSRKRK LLLHKNEIQY LCNKKNKIGS TLVALSLFWE KSWCKLNFGL AKGKTKIDKR ASEKQNEWKK EKLKILKKVK FQN //