SSRP_PROMS
ID SSRP_PROMS Reviewed; 164 AA.
AC A2BTJ8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, 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=A9601_18261;
OS Prochlorococcus marinus (strain AS9601).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=146891;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS9601;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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; CP000551; ABM71109.1; -; Genomic_DNA.
DR RefSeq; WP_011819228.1; NC_008816.1.
DR AlphaFoldDB; A2BTJ8; -.
DR SMR; A2BTJ8; -.
DR STRING; 146891.A9601_18261; -.
DR EnsemblBacteria; ABM71109; ABM71109; A9601_18261.
DR KEGG; pmb:A9601_18261; -.
DR eggNOG; COG0691; Bacteria.
DR HOGENOM; CLU_108953_0_1_3; -.
DR OMA; WTNHSAR; -.
DR OrthoDB; 1720952at2; -.
DR Proteomes; UP000002590; 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..164
FT /note="SsrA-binding protein"
FT /id="PRO_0000331075"
FT REGION 141..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 164 AA; 18717 MW; AFBD0A034FFA0B79 CRC64;
MAKNSNKVKK NTNKANNFKL LADNRYAKFQ YAISETIEAG IELLGTEVKS IRNGKANLRD
GYCSFRDGEI LLLNVHISPH KNVGSFFNHD PLRNRKLLLH KKEIIKMKSN TEKKGMTIVP
LSLYLKGSWI KLTIGVGKGK KLHDKRQDEK QKSIKKEINS ALKR