SSRP_MYCCT
ID SSRP_MYCCT Reviewed; 148 AA.
AC Q2ST23;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=MCAP_0096;
OS Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS / NCTC 10154).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=340047;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000123; ABC01243.1; -; Genomic_DNA.
DR RefSeq; WP_011386995.1; NC_007633.1.
DR AlphaFoldDB; Q2ST23; -.
DR SMR; Q2ST23; -.
DR EnsemblBacteria; ABC01243; ABC01243; MCAP_0096.
DR GeneID; 23778949; -.
DR KEGG; mcp:MCAP_0096; -.
DR HOGENOM; CLU_108953_0_1_14; -.
DR OMA; WTNHSAR; -.
DR OrthoDB; 1720952at2; -.
DR PhylomeDB; Q2ST23; -.
DR Proteomes; UP000001928; 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; RNA-binding.
FT CHAIN 1..148
FT /note="SsrA-binding protein"
FT /id="PRO_1000002085"
SQ SEQUENCE 148 AA; 17761 MW; 4BB35058672AF095 CRC64;
MSEHLIVKNK KAYFNYEIIQ TYQAGIVLNG PEIKSIRNHD VSINEAFVLI RKKEIYILNM
NVKKYQFANY IKGLEETRTR KLLLHKKEII KILNKIKQEN LTIIPIKLYF KNDYVKLEIA
LAKGKKLHDK RQTIKKRDTE RKELRDYK