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SSRP_SINMW
ID   SSRP_SINMW              Reviewed;         159 AA.
AC   A6U7A0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=Smed_0674;
OS   Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=366394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM419;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA   Richardson P.;
RT   "Complete sequence of Sinorhizobium medicae WSM419 chromosome.";
RL   Submitted (JUN-2007) 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; CP000738; ABR59530.1; -; Genomic_DNA.
DR   RefSeq; WP_011974876.1; NC_009636.1.
DR   RefSeq; YP_001326365.1; NC_009636.1.
DR   AlphaFoldDB; A6U7A0; -.
DR   SMR; A6U7A0; -.
DR   STRING; 366394.Smed_0674; -.
DR   PRIDE; A6U7A0; -.
DR   EnsemblBacteria; ABR59530; ABR59530; Smed_0674.
DR   GeneID; 61609950; -.
DR   KEGG; smd:Smed_0674; -.
DR   PATRIC; fig|366394.8.peg.3776; -.
DR   eggNOG; COG0691; Bacteria.
DR   HOGENOM; CLU_108953_0_1_5; -.
DR   OMA; WTNHSAR; -.
DR   OrthoDB; 1720952at2; -.
DR   Proteomes; UP000001108; 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..159
FT                   /note="SsrA-binding protein"
FT                   /id="PRO_1000002151"
FT   REGION          133..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   159 AA;  18558 MW;  8C800F5D19A3483B CRC64;
     MAPKGSERTV KKVVAENRKA RFNYEIVDTY EAGLVLTGTE VKSLREGKAN IAESYATDEG
     GEIWLINSYL PEYLQANRFN HETRRRRKLL LSRREVNRLQ GAVNREGMSL IPLRIYFNER
     GRAKLELALG KGKKLHDKRE TSKERDWNRQ KNRLLKERG
 
 
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