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SSRP_CORU7
ID   SSRP_CORU7              Reviewed;         178 AA.
AC   B1VI76;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=cu1500;
OS   Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=504474;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43042 / DSM 7109;
RX   PubMed=18367281; DOI=10.1016/j.jbiotec.2008.02.009;
RA   Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A.,
RA   Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., Kalinowski J.,
RA   Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., Soriano F., Droege M.,
RA   Puehler A.;
RT   "The lifestyle of Corynebacterium urealyticum derived from its complete
RT   genome sequence established by pyrosequencing.";
RL   J. Biotechnol. 136:11-21(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. 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; AM942444; CAQ05460.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1VI76; -.
DR   SMR; B1VI76; -.
DR   STRING; 504474.cu1500; -.
DR   EnsemblBacteria; CAQ05460; CAQ05460; cu1500.
DR   KEGG; cur:cu1500; -.
DR   eggNOG; COG0691; Bacteria.
DR   HOGENOM; CLU_108953_2_1_11; -.
DR   OMA; WTNHSAR; -.
DR   OrthoDB; 1720952at2; -.
DR   Proteomes; UP000001727; 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..178
FT                   /note="SsrA-binding protein"
FT                   /id="PRO_1000090143"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   178 AA;  20098 MW;  0B14F2D0618B37B1 CRC64;
     MAKKSTPVDS GRSKGKKASA PRGGGPAVIA TNRKARHDYH ILDTYECGVV LVGTEVKALR
     EGKASLVDAY ATIDAGEVWL RGLHIPEYSR GNFWNHTPRR VRKLLLHRRE IDSLTGKVRD
     GNHTLVPLQL YFVDGRLKCE LALARGKQDY DKRQDIKRRT EEREVVRELG RKIKGMKG
 
 
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