RS11_MYCMM
ID RS11_MYCMM Reviewed; 138 AA.
AC B2HCX2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=30S ribosomal protein S11 {ECO:0000255|HAMAP-Rule:MF_01310};
GN Name=rpsK {ECO:0000255|HAMAP-Rule:MF_01310}; OrderedLocusNames=MMAR_1088;
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=216594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M;
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(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; CP000854; ACC39544.1; -; Genomic_DNA.
DR RefSeq; WP_011739107.1; NC_010612.1.
DR AlphaFoldDB; B2HCX2; -.
DR SMR; B2HCX2; -.
DR STRING; 216594.MMAR_1088; -.
DR EnsemblBacteria; ACC39544; ACC39544; MMAR_1088.
DR GeneID; 64259830; -.
DR KEGG; mmi:MMAR_1088; -.
DR eggNOG; COG0100; Bacteria.
DR HOGENOM; CLU_072439_5_0_11; -.
DR OMA; KWGVAHI; -.
DR OrthoDB; 1713391at2; -.
DR Proteomes; UP000001190; 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..138
FT /note="30S ribosomal protein S11"
FT /id="PRO_1000141114"
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