ID   RS11_SACEN              Reviewed;         134 AA.
AC   A4FPJ4;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=30S ribosomal protein S11 {ECO:0000255|HAMAP-Rule:MF_01310};
GN   Name=rpsK {ECO:0000255|HAMAP-Rule:MF_01310}; OrderedLocusNames=SACE_6805;
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS   NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC   2338;
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA   Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
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; AM420293; CAM05969.1; -; Genomic_DNA.
DR   RefSeq; WP_009948668.1; NZ_PDBV01000001.1.
DR   AlphaFoldDB; A4FPJ4; -.
DR   SMR; A4FPJ4; -.
DR   STRING; 405948.SACE_6805; -.
DR   EnsemblBacteria; CAM05969; CAM05969; SACE_6805.
DR   KEGG; sen:SACE_6805; -.
DR   eggNOG; COG0100; Bacteria.
DR   HOGENOM; CLU_072439_5_0_11; -.
DR   OMA; KWGVAHI; -.
DR   OrthoDB; 1713391at2; -.
DR   Proteomes; UP000006728; Chromosome.
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   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..134
FT                   /note="30S ribosomal protein S11"
FT                   /id="PRO_0000294846"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          115..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..22
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   134 AA;  14272 MW;  77CF4B3C2B202D9F CRC64;
     MPPKSRAGAV KKVRRKEKKN VAHGQAHIKS TFNNTIVSIT DPTGAVISWA SAGHVGFKGS
     RKSTPFAAQM AAENAARKAA EHGMKKVDVF VKGPGSGRET AIRSLQAAGL EVGTIQDVTP
     QPHNGCRPPK RRRV