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RS15_ACIC1
ID   RS15_ACIC1              Reviewed;          89 AA.
AC   A0LV21;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=30S ribosomal protein S15 {ECO:0000255|HAMAP-Rule:MF_01343};
GN   Name=rpsO {ECO:0000255|HAMAP-Rule:MF_01343}; OrderedLocusNames=Acel_1509;
OS   Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC   Bacteria; Actinobacteria; Acidothermales; Acidothermaceae; Acidothermus.
OX   NCBI_TaxID=351607;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43068 / DSM 8971 / 11B;
RX   PubMed=19270083; DOI=10.1101/gr.084848.108;
RA   Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA   Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA   Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT   "Complete genome of the cellulolytic thermophile Acidothermus
RT   cellulolyticus 11B provides insights into its ecophysiological and
RT   evolutionary adaptations.";
RL   Genome Res. 19:1033-1043(2009).
CC   -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC       to 16S rRNA where it helps nucleate assembly of the platform of the 30S
CC       subunit by binding and bridging several RNA helices of the 16S rRNA.
CC       {ECO:0000255|HAMAP-Rule:MF_01343}.
CC   -!- FUNCTION: Forms an intersubunit bridge (bridge B4) with the 23S rRNA of
CC       the 50S subunit in the ribosome. {ECO:0000255|HAMAP-Rule:MF_01343}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a bridge to the 50S
CC       subunit in the 70S ribosome, contacting the 23S rRNA.
CC       {ECO:0000255|HAMAP-Rule:MF_01343}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS15 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01343}.
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DR   EMBL; CP000481; ABK53281.1; -; Genomic_DNA.
DR   RefSeq; WP_011720344.1; NC_008578.1.
DR   AlphaFoldDB; A0LV21; -.
DR   SMR; A0LV21; -.
DR   STRING; 351607.Acel_1509; -.
DR   PRIDE; A0LV21; -.
DR   EnsemblBacteria; ABK53281; ABK53281; Acel_1509.
DR   KEGG; ace:Acel_1509; -.
DR   eggNOG; COG0184; Bacteria.
DR   HOGENOM; CLU_148518_0_0_11; -.
DR   OMA; FKTHVKD; -.
DR   OrthoDB; 1990141at2; -.
DR   Proteomes; UP000008221; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00353; Ribosomal_S15p_S13e; 1.
DR   HAMAP; MF_01343_B; Ribosomal_S15_B; 1.
DR   InterPro; IPR000589; Ribosomal_S15.
DR   InterPro; IPR005290; Ribosomal_S15_bac-type.
DR   InterPro; IPR009068; S15_NS1_RNA-bd.
DR   PANTHER; PTHR23321; PTHR23321; 1.
DR   Pfam; PF00312; Ribosomal_S15; 1.
DR   SMART; SM01387; Ribosomal_S15; 1.
DR   SUPFAM; SSF47060; SSF47060; 1.
DR   TIGRFAMs; TIGR00952; S15_bact; 1.
DR   PROSITE; PS00362; RIBOSOMAL_S15; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..89
FT                   /note="30S ribosomal protein S15"
FT                   /id="PRO_1000054738"
SQ   SEQUENCE   89 AA;  10382 MW;  00B2D002BF9F7A5A CRC64;
     MALDTATKRS ILAEYATTEG DTGSPEVQVA LLTRRITDLT EHLKVHRHDH HSRRGLLLLV
     GRRRRLLRYL AKKDIARYRS LIERLGLRR
 
 
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