ID   SSRP_UREPA              Reviewed;         141 AA.
AC   Q9PR87;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 99.
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=UU058;
OS   Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX   NCBI_TaxID=273119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700970;
RX   PubMed=11048724; DOI=10.1038/35037619;
RA   Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA   Cassell G.H.;
RT   "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL   Nature 407:757-762(2000).
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; AF222894; AAF30463.1; -; Genomic_DNA.
DR   RefSeq; WP_006688578.1; NC_002162.1.
DR   AlphaFoldDB; Q9PR87; -.
DR   SMR; Q9PR87; -.
DR   STRING; 273119.UU058; -.
DR   EnsemblBacteria; AAF30463; AAF30463; UU058.
DR   GeneID; 29672291; -.
DR   KEGG; uur:UU058; -.
DR   eggNOG; COG0691; Bacteria.
DR   HOGENOM; CLU_108953_0_1_14; -.
DR   OMA; WTNHSAR; -.
DR   Proteomes; UP000000423; 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..141
FT                   /note="SsrA-binding protein"
FT                   /id="PRO_0000103062"
SQ   SEQUENCE   141 AA;  16700 MW;  C4A9AC71EA7EB712 CRC64;
     MIVSNKHARR NYELLDFFEC GIVLKGTEVK SISRANCSIN EAYVQIIKNQ ALILNMHVAN
     FFEGNNFNQD PYRNRKLLLH KKEIIRLQHL VKTQHMTIVP TKIYWKNNKL KIEIALGKGK
     QLHDKREDIK KRDLARETRL F