ID   RS11_MYCUA              Reviewed;         138 AA.
AC   A0PMB5;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=30S ribosomal protein S11 {ECO:0000255|HAMAP-Rule:MF_01310};
GN   Name=rpsK {ECO:0000255|HAMAP-Rule:MF_01310}; OrderedLocusNames=MUL_0846;
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=362242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99;
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA   Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA   Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(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; CP000325; ABL03484.1; -; Genomic_DNA.
DR   RefSeq; WP_011739107.1; NC_008611.1.
DR   AlphaFoldDB; A0PMB5; -.
DR   SMR; A0PMB5; -.
DR   STRING; 362242.MUL_0846; -.
DR   EnsemblBacteria; ABL03484; ABL03484; MUL_0846.
DR   GeneID; 64259830; -.
DR   KEGG; mul:MUL_0846; -.
DR   eggNOG; COG0100; Bacteria.
DR   HOGENOM; CLU_072439_5_0_11; -.
DR   OMA; KWGVAHI; -.
DR   Proteomes; UP000000765; 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   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..138
FT                   /note="30S ribosomal protein S11"
FT                   /id="PRO_0000294800"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..26
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   138 AA;  14686 MW;  A88D3107DD3197AE CRC64;
     MPPKKASGTG PKKGQKTRRR EKKNVPHGAA HIKSTFNNTI VTITDPQGNV IAWASSGHVG
     FKGSRKSTPF AAQLAAENAA RKAQEHGVRK VDVFVKGPGS GRETAIRSLQ AAGLEVGAIS
     DVTPQPHNGV RPPKRRRV