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SSRP_SPHEL
ID   SSRP_SPHEL              Reviewed;         160 AA.
AC   Q7X2N6;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   23-FEB-2022, entry version 57.
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};
OS   Sphingomonas elodea.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=179878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31461 / PS-60;
RA   Harding N.E., Patel Y.N., Coleman R.J.;
RT   "Genes required for gellan polysaccharide biosynthesis in Sphingomonas
RT   elodea ATCC31461.";
RL   Submitted (JAN-2003) 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; AY220100; AAP46182.1; -; Genomic_DNA.
DR   STRING; 1081640.AGFU01000061_gene239; -.
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..160
FT                   /note="SsrA-binding protein"
FT                   /id="PRO_0000103027"
SQ   SEQUENCE   160 AA;  18471 MW;  8970084FE21BD5F9 CRC64;
     MARPRPATFD KVKTVAENRR ARFDYFIEQT YEAGLVLTGT EVKSLRFGEG SIAEAYAEVK
     DEXVWLVNAN IPEFSHGNRF NHEAKRPRKL LLHEREINKL HGAVAREGMT LVPLSVYFNG
     KGRAKVELAL AKGKKTHDKR ETIKERDWKR EQSRILRDRG
 
 
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