ID U7TAQ3_FUSNU Unreviewed; 148 AA. AC U7TAQ3; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 03-JUL-2019, entry version 29. DE RecName: Full=SsrA-binding protein {ECO:0000256|HAMAP-Rule:MF_00023, ECO:0000256|SAAS:SAAS00732293}; DE AltName: Full=Small protein B {ECO:0000256|HAMAP-Rule:MF_00023}; GN Name=smpB {ECO:0000256|HAMAP-Rule:MF_00023}; GN ORFNames=HMPREF1538_01489 {ECO:0000313|EMBL:ERT41007.1}; OS Fusobacterium nucleatum CTI-1. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=1204474 {ECO:0000313|EMBL:ERT41007.1, ECO:0000313|Proteomes:UP000017136}; RN [1] {ECO:0000313|EMBL:ERT41007.1, ECO:0000313|Proteomes:UP000017136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CTI-1 {ECO:0000313|EMBL:ERT41007.1, RC ECO:0000313|Proteomes:UP000017136}; RG The Broad Institute Genomics Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Kostic A., Garrett W., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., RA Alvarado L., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J., RA Gnerre S., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., RA Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium nucleatum CTI-1."; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Required for rescue of stalled ribosomes mediated by CC trans-translation. Binds to transfer-messenger RNA (tmRNA), CC required for stable association of tmRNA with ribosomes. tmRNA and CC SmpB together mimic tRNA shape, replacing the anticodon stem-loop CC with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold CC to resemble tRNA(Ala) and it encodes a "tag peptide", a short CC internal open reading frame. During trans-translation Ala- CC aminoacylated tmRNA acts like a tRNA, entering the A-site of CC stalled ribosomes, displacing the stalled mRNA. The ribosome then CC switches to translate the ORF on the tmRNA; the nascent peptide is CC 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:0000256|HAMAP-Rule:MF_00023}. CC -!- FUNCTION: Required for rescue of stalled ribosomes mediated by CC trans-translation. Binds to transfer-messenger RNA (tmRNA), CC required for stable association of tmRNA with ribosomes. tmRNA and CC SmpB together mimic tRNA shape, replacing the anticodon stem-loop CC with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold CC to resemble tRNA(Ala) and it encodes a 'tag peptide', a short CC internal open reading frame. During trans-translation Ala- CC aminoacylated tmRNA acts like a tRNA, entering the A-site of CC stalled ribosomes, displacing the stalled mRNA. The ribosome then CC switches to translate the ORF on the tmRNA; the nascent peptide is CC 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:0000256|SAAS:SAAS00732441}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00023}. CC Note=The tmRNA-SmpB complex associates with stalled 70S ribosomes. CC {ECO:0000256|HAMAP-Rule:MF_00023}. CC -!- SIMILARITY: Belongs to the SmpB family. {ECO:0000256|HAMAP- CC Rule:MF_00023, ECO:0000256|SAAS:SAAS00732332}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERT41007.1}. 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; AXNZ01000016; ERT41007.1; -; Genomic_DNA. DR RefSeq; WP_023040117.1; NZ_KI518461.1. DR EnsemblBacteria; ERT41007; ERT41007; HMPREF1538_01489. DR PATRIC; fig|1204474.3.peg.1454; -. DR BioCyc; GCF_000479285-HMP:HMPREF1538_RS04065-MONOMER; -. DR Proteomes; UP000017136; Unassembled WGS sequence. 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 PANTHER; PTHR30308; PTHR30308; 1. DR Pfam; PF01668; SmpB; 1. DR SUPFAM; SSF74982; SSF74982; 1. DR TIGRFAMs; TIGR00086; smpB; 1. DR PROSITE; PS01317; SSRP; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017136}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00023, KW ECO:0000256|SAAS:SAAS00732411}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00023, KW ECO:0000256|SAAS:SAAS00732379}. FT REGION 128 148 Disordered. {ECO:0000256|MobiDB-lite: FT U7TAQ3}. SQ SEQUENCE 148 AA; 17359 MW; C5B5C424707730A2 CRC64; MIIANNKKAF FDYFIEEKYE AGIELKGSEV KSIKAGKVSI KESFVRIIND EIFIMGMSVV PWDFGSVYNP EERRVRKLLL HRKEIKKIHE KVKIKGYTIV PLDVHLSKGY VKIQIAIAKG KKTYDKRESI AKKDQERNLK REFKNNNR //