SSRP_HELPY
ID SSRP_HELPY Reviewed; 152 AA.
AC O25985;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 114.
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=HP_1444;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP INDUCTION BY ACID STRESS.
RX PubMed=15228539; DOI=10.1111/j.1365-2958.2004.04137.x;
RA Bury-Mone S., Thiberge J.M., Contreras M., Maitournam A., Labigne A.,
RA De Reuse H.;
RT "Responsiveness to acidity via metal ion regulators mediates virulence in
RT the gastric pathogen Helicobacter pylori.";
RL Mol. Microbiol. 53:623-638(2004).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700392 / 26695, N6, and X47-2AL;
RX PubMed=19043582; DOI=10.1371/journal.pone.0003810;
RA Thibonnier M., Thiberge J.M., De Reuse H.;
RT "Trans-translation in Helicobacter pylori: essentiality of ribosome rescue
RT and requirement of protein tagging for stress resistance and competence.";
RL PLoS ONE 3:E3810-E3810(2008).
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 (Probable). tmRNA and SmpB
CC together mimic tRNA shape, replacing the anticodon stem-loop with SmpB.
CC tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble
CC tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading
CC frame. During trans-translation Ala-aminoacylated tmRNA acts like a
CC tRNA, entering the A-site of stalled ribosomes, displacing the stalled
CC mRNA. 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 (PubMed:19043582). {ECO:0000255|HAMAP-Rule:MF_00023,
CC ECO:0000269|PubMed:19043582}.
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 -!- INDUCTION: By growth at pH 5.0 in exponential phase.
CC {ECO:0000269|PubMed:15228539}.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted. Depletion
CC experiments show loss of growth after 12 hours, cells remain viable for
CC a further 12 hours before they can no longer be rescued by induction of
CC smpB. Similarly, the gene for tmRNA (ssrA) cannot be deleted; mutations
CC in the tmRNA show that it is the ribosome rescue function and not
CC protein tagging and subsequent degradation that is essential for
CC viability. Mutant tmRNAs that affect protein tagging are however more
CC susceptible to antibiotic stress and less naturally competent for DNA
CC transformation. {ECO:0000269|PubMed:19043582}.
CC -!- SIMILARITY: Belongs to the SmpB family. {ECO:0000255|HAMAP-
CC Rule:MF_00023}.
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DR EMBL; AE000511; AAD08482.1; -; Genomic_DNA.
DR PIR; D64700; D64700.
DR RefSeq; NP_208235.1; NC_000915.1.
DR RefSeq; WP_000766480.1; NC_018939.1.
DR AlphaFoldDB; O25985; -.
DR SMR; O25985; -.
DR DIP; DIP-3736N; -.
DR IntAct; O25985; 10.
DR MINT; O25985; -.
DR STRING; 85962.C694_07480; -.
DR PaxDb; O25985; -.
DR EnsemblBacteria; AAD08482; AAD08482; HP_1444.
DR KEGG; hpy:HP_1444; -.
DR PATRIC; fig|85962.47.peg.1553; -.
DR eggNOG; COG0691; Bacteria.
DR OMA; WTNHSAR; -.
DR PhylomeDB; O25985; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0070929; P:trans-translation; IEA:UniProtKB-UniRule.
DR GO; GO:0070930; P:trans-translation-dependent protein tagging; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cytoplasm; Reference proteome; RNA-binding; Stress response.
FT CHAIN 1..152
FT /note="SsrA-binding protein"
FT /id="PRO_0000102960"
SQ SEQUENCE 152 AA; 17824 MW; 2CD90E775CE6C360 CRC64;
MKLIASNKKA YFDYEILETL EAGLALLGSE VKALRQTRVN LKDNFVKIIK GEAFLFGVHI
SYLDTIHAYY KPNERRERKL LLHKKQLLKW QIEASKERLS IVGLKLYFNQ RNRAKIQIAL
VKGKRLHDKR QSLKEKALNK EILADLKHHF KG
