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RS11_CUPTR
ID   RS11_CUPTR              Reviewed;         132 AA.
AC   B3R7E5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=30S ribosomal protein S11 {ECO:0000255|HAMAP-Rule:MF_01310};
GN   Name=rpsK {ECO:0000255|HAMAP-Rule:MF_01310}; OrderedLocusNames=RALTA_A2920;
OS   Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS   107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=977880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 / R1;
RX   PubMed=18490699; DOI=10.1101/gr.076448.108;
RA   Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA   Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA   Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA   Masson-Boivin C.;
RT   "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT   comparative genomics of rhizobia.";
RL   Genome Res. 18:1472-1483(2008).
CC   -!- FUNCTION: Located on the platform of the 30S subunit, it bridges
CC       several disparate RNA helices of the 16S rRNA. Forms part of the Shine-
CC       Dalgarno cleft in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01310}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Interacts with proteins S7
CC       and S18. Binds to IF-3. {ECO:0000255|HAMAP-Rule:MF_01310}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS11 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01310}.
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DR   EMBL; CU633749; CAQ70845.1; -; Genomic_DNA.
DR   RefSeq; WP_010812376.1; NC_010528.1.
DR   AlphaFoldDB; B3R7E5; -.
DR   SMR; B3R7E5; -.
DR   STRING; 977880.RALTA_A2920; -.
DR   EnsemblBacteria; CAQ70845; CAQ70845; RALTA_A2920.
DR   GeneID; 57645590; -.
DR   KEGG; cti:RALTA_A2920; -.
DR   eggNOG; COG0100; Bacteria.
DR   HOGENOM; CLU_072439_5_0_4; -.
DR   OMA; KWGVAHI; -.
DR   OrthoDB; 1713391at2; -.
DR   BioCyc; CTAI977880:RALTA_RS14235-MON; -.
DR   Proteomes; UP000001692; Chromosome 1.
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   Gene3D; 3.30.420.80; -; 1.
DR   HAMAP; MF_01310; Ribosomal_S11; 1.
DR   InterPro; IPR001971; Ribosomal_S11.
DR   InterPro; IPR019981; Ribosomal_S11_bac-type.
DR   InterPro; IPR018102; Ribosomal_S11_CS.
DR   InterPro; IPR036967; Ribosomal_S11_sf.
DR   PANTHER; PTHR11759; PTHR11759; 1.
DR   Pfam; PF00411; Ribosomal_S11; 1.
DR   PIRSF; PIRSF002131; Ribosomal_S11; 1.
DR   TIGRFAMs; TIGR03632; uS11_bact; 1.
DR   PROSITE; PS00054; RIBOSOMAL_S11; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..132
FT                   /note="30S ribosomal protein S11"
FT                   /id="PRO_1000141078"
SQ   SEQUENCE   132 AA;  13977 MW;  E38756566B0D5D7F CRC64;
     MAKGPNNAAR ARKKVKKNVA DGIAHVHASF NNTIITITDR QGNALSWATA GGQGFKGSRK
     STPFAAQVAA ENAGRVAQDQ GIKNLEVRIK GPGPGRESAV RALNALGIKI AIIEDVTPIP
     HNGCRPPKRR RI
 
 
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