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SSRP_BRADU
ID   SSRP_BRADU              Reviewed;         157 AA.
AC   Q9RH74; Q89K47;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 2.
DT   25-MAY-2022, entry version 106.
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=bll5070;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=USDA 110spc4;
RA   Mueller P., Stingel D.;
RT   "Extended DNA sequencing in the upstream region of sipF in Bradyrhizobium
RT   japonicum.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
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; AF065159; AAF04322.1; -; Genomic_DNA.
DR   EMBL; BA000040; BAC50335.1; -; Genomic_DNA.
DR   RefSeq; NP_771710.1; NC_004463.1.
DR   RefSeq; WP_011087830.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q9RH74; -.
DR   SMR; Q9RH74; -.
DR   STRING; 224911.27353335; -.
DR   EnsemblBacteria; BAC50335; BAC50335; BAC50335.
DR   GeneID; 64024834; -.
DR   KEGG; bja:bll5070; -.
DR   PATRIC; fig|224911.44.peg.4938; -.
DR   eggNOG; COG0691; Bacteria.
DR   HOGENOM; CLU_108953_0_1_5; -.
DR   InParanoid; Q9RH74; -.
DR   OMA; WTNHSAR; -.
DR   PhylomeDB; Q9RH74; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0070929; P:trans-translation; IEA:UniProtKB-UniRule.
DR   GO; GO:0070930; P:trans-translation-dependent protein tagging; IBA:GO_Central.
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..157
FT                   /note="SsrA-binding protein"
FT                   /id="PRO_0000102917"
FT   REGION          133..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..152
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        100
FT                   /note="A -> P (in Ref. 1; AAF04322)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        117
FT                   /note="E -> G (in Ref. 1; AAF04322)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        146..154
FT                   /note="SREKGRLLR -> EPGRRSACCG (in Ref. 1; AAF04322)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   157 AA;  18135 MW;  8FF2DF48EB46B73D CRC64;
     MADKNERPIK VMAENRKARF NYAIEDTIEA GIALTGTEVK SIRNGKSTIA ESYADSKNGE
     IWLINATIPE YLQGNRFNHE PKRPRKLLLH RRQINKLIGA VDREGMTLIP LKLYFNERGR
     AKLQLAVAKG KKLHDKRETE KKRDWSREKG RLLRARG
 
 
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