SSRP_BURTA
ID SSRP_BURTA Reviewed; 148 AA.
AC Q2SWX6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=BTH_I2049;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
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; CP000086; ABC38002.1; -; Genomic_DNA.
DR RefSeq; WP_006026082.1; NZ_CP008785.1.
DR AlphaFoldDB; Q2SWX6; -.
DR SMR; Q2SWX6; -.
DR PRIDE; Q2SWX6; -.
DR EnsemblBacteria; ABC38002; ABC38002; BTH_I2049.
DR GeneID; 66547463; -.
DR KEGG; bte:BTH_I2049; -.
DR HOGENOM; CLU_108953_3_0_4; -.
DR OMA; WTNHSAR; -.
DR OrthoDB; 1720952at2; -.
DR Proteomes; UP000001930; Chromosome I.
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; RNA-binding.
FT CHAIN 1..148
FT /note="SsrA-binding protein"
FT /id="PRO_1000002020"
FT REGION 123..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 148 AA; 17189 MW; 5AC62B40598BC79B CRC64;
MSIIDNRKAF FDYHIEERYE AGLVLEGWEV KALRAGRGQI KEGYVVVKNA EIFLIGTHIS
PLPEASTHIK PDPVRTRKLL LHRDEIKKLI GKVEQRGYTL VPLNFHYKGG RVKCEIGLAK
GKKLHDKRET EKKRDWEREK ARIMRSAT