SSRP_GLUOX
ID SSRP_GLUOX Reviewed; 164 AA.
AC Q5FUX0;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-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=GOX0060;
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H;
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(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; CP000009; AAW59857.1; -; Genomic_DNA.
DR RefSeq; WP_011251661.1; NZ_LT900338.1.
DR AlphaFoldDB; Q5FUX0; -.
DR SMR; Q5FUX0; -.
DR STRING; 290633.GOX0060; -.
DR EnsemblBacteria; AAW59857; AAW59857; GOX0060.
DR GeneID; 56904311; -.
DR KEGG; gox:GOX0060; -.
DR eggNOG; COG0691; Bacteria.
DR HOGENOM; CLU_108953_0_1_5; -.
DR OMA; WTNHSAR; -.
DR Proteomes; UP000006375; 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..164
FT /note="SsrA-binding protein"
FT /id="PRO_0000102955"
SQ SEQUENCE 164 AA; 18364 MW; 73980BB6F2168297 CRC64;
MAGKKTKSGM ISHGMAAQNR KGRFDYTILE TTEAGIVLKG PEVKSLRLGR ATITEAYAAE
RDGEIWLFNS YIPEYQGGVL SRFEPRAPRK LLMHRKQIAH FLGAVSRAGA SLVPLDIHFN
ARGMAKVTLG LGQGRRKEDK RHAIAERDWK RDKARLVRSS GKDY