SSRP_PAEAT
ID SSRP_PAEAT Reviewed; 156 AA.
AC A1R807;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 102.
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}; OrderedLocusNames=AAur_2653;
OS Paenarthrobacter aurescens (strain TC1).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Paenarthrobacter.
OX NCBI_TaxID=290340;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC1;
RX PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V.,
RA Khouri H.M., Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT "Secrets of soil survival revealed by the genome sequence of Arthrobacter
RT aurescens TC1.";
RL PLoS Genet. 2:2094-2106(2006).
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}.
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DR EMBL; CP000474; ABM07752.1; -; Genomic_DNA.
DR RefSeq; WP_011775311.1; NC_008711.1.
DR AlphaFoldDB; A1R807; -.
DR SMR; A1R807; -.
DR STRING; 290340.AAur_2653; -.
DR EnsemblBacteria; ABM07752; ABM07752; AAur_2653.
DR KEGG; aau:AAur_2653; -.
DR eggNOG; COG0691; Bacteria.
DR HOGENOM; CLU_108953_2_1_11; -.
DR OMA; WTNHSAR; -.
DR OrthoDB; 1720952at2; -.
DR Proteomes; UP000000637; 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 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 Cytoplasm; Reference proteome; RNA-binding.
FT CHAIN 1..156
FT /note="SsrA-binding protein"
FT /id="PRO_1000001994"
FT REGION 134..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 156 AA; 18468 MW; 15EAA39402F0748E CRC64;
MPKESGRKVV ATNRKARHNY HVMDTYEAGI ALMGTEVKSL REGHASMVDG FCTFYNDELW
MEGIHIPEYH QGSWTNHAAR RRRKLLLHRD ELDKISQKIR ESGFTVVPLQ LYFLDGRAKV
EIAIARGKKD YDKRQTLREQ QDKRESLREL RERNRR