(data stored in ACNUC7421 zone)

SWISSPROT: A0A0F6BIL2_GEOS0

ID   A0A0F6BIL2_GEOS0        Unreviewed;       155 AA.
AC   A0A0F6BIL2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   16-JAN-2019, entry version 24.
DE   RecName: Full=SsrA-binding protein {ECO:0000256|HAMAP-Rule:MF_00023, ECO:0000256|SAAS:SAAS00732293};
DE   AltName: Full=Small protein B {ECO:0000256|HAMAP-Rule:MF_00023};
GN   Name=smpB {ECO:0000256|HAMAP-Rule:MF_00023};
GN   OrderedLocusNames=GY4MC1_0423 {ECO:0000313|EMBL:ADP73263.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73263.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73263.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73263.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for rescue of stalled ribosomes mediated by
CC       trans-translation. Binds to transfer-messenger RNA (tmRNA),
CC       required for stable association of tmRNA with ribosomes. tmRNA and
CC       SmpB together mimic tRNA shape, replacing the anticodon stem-loop
CC       with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold
CC       to resemble tRNA(Ala) and it encodes a "tag peptide", a short
CC       internal open reading frame. During trans-translation Ala-
CC       aminoacylated tmRNA acts like a tRNA, entering the A-site of
CC       stalled ribosomes, displacing the stalled mRNA. The ribosome then
CC       switches to translate the ORF on the tmRNA; the nascent peptide is
CC       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:0000256|HAMAP-Rule:MF_00023}.
CC   -!- FUNCTION: Required for rescue of stalled ribosomes mediated by
CC       trans-translation. Binds to transfer-messenger RNA (tmRNA),
CC       required for stable association of tmRNA with ribosomes. tmRNA and
CC       SmpB together mimic tRNA shape, replacing the anticodon stem-loop
CC       with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold
CC       to resemble tRNA(Ala) and it encodes a 'tag peptide', a short
CC       internal open reading frame. During trans-translation Ala-
CC       aminoacylated tmRNA acts like a tRNA, entering the A-site of
CC       stalled ribosomes, displacing the stalled mRNA. The ribosome then
CC       switches to translate the ORF on the tmRNA; the nascent peptide is
CC       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:0000256|SAAS:SAAS00732441}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00023}.
CC       Note=The tmRNA-SmpB complex associates with stalled 70S ribosomes.
CC       {ECO:0000256|HAMAP-Rule:MF_00023}.
CC   -!- SIMILARITY: Belongs to the SmpB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00023, ECO:0000256|SAAS:SAAS00732332}.
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DR   EMBL; CP002293; ADP73263.1; -; Genomic_DNA.
DR   RefSeq; WP_003248121.1; NC_014650.1.
DR   EnsemblBacteria; ADP73263; ADP73263; GY4MC1_0423.
DR   GeneID; 29236917; -.
DR   KEGG; gmc:GY4MC1_0423; -.
DR   KO; K03664; -.
DR   OMA; KLHDKRA; -.
DR   OrthoDB; 1720952at2; -.
DR   BioCyc; GSP581103:G1GOQ-470-MONOMER; -.
DR   Proteomes; UP000002034; 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   ProDom; PD004488; SmpB; 1.
DR   SUPFAM; SSF74982; SSF74982; 1.
DR   TIGRFAMs; TIGR00086; smpB; 1.
DR   PROSITE; PS01317; SSRP; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BIL2.
DR   SWISS-2DPAGE; A0A0F6BIL2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00023,
KW   ECO:0000256|SAAS:SAAS00732411};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00023,
KW   ECO:0000256|SAAS:SAAS00732379}.
SQ   SEQUENCE   155 AA;  18166 MW;  06F87C4F1DA3CCFF CRC64;
     MPKGEGKLIA QNKKAHHDYF IEETYEAGIV LKGTEIKSIR AGKVNLKDSF AKVEKGEVFL
     HNMHISPYEQ GNRYNHDPLR TRKLLLHRRE INKLIGYTKE QGYTLVPIKL YIKNGFAKVL
     LGVGKGKKKY DKREDMKRKE AQREIERAFR ERQKI
//

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