RS11_MYCLE
ID RS11_MYCLE Reviewed; 138 AA.
AC Q9X7A0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=30S ribosomal protein S11 {ECO:0000255|HAMAP-Rule:MF_01310};
GN Name=rpsK {ECO:0000255|HAMAP-Rule:MF_01310}; OrderedLocusNames=ML1959;
GN ORFNames=MLCB1222.29c;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; AL049491; CAB39835.1; -; Genomic_DNA.
DR EMBL; AL583923; CAC30914.1; -; Genomic_DNA.
DR PIR; B87154; B87154.
DR RefSeq; NP_302324.1; NC_002677.1.
DR RefSeq; WP_010908645.1; NC_002677.1.
DR AlphaFoldDB; Q9X7A0; -.
DR SMR; Q9X7A0; -.
DR STRING; 272631.ML1959; -.
DR EnsemblBacteria; CAC30914; CAC30914; CAC30914.
DR KEGG; mle:ML1959; -.
DR PATRIC; fig|272631.5.peg.3709; -.
DR Leproma; ML1959; -.
DR eggNOG; COG0100; Bacteria.
DR HOGENOM; CLU_072439_5_0_11; -.
DR OMA; KWGVAHI; -.
DR Proteomes; UP000000806; 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_0000123178"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 138 AA; 14747 MW; 02620172835D0B00 CRC64;
MPPKKANAAG PKKGQKTRKR EKKNIPYGAA HIKSTFNNTI VTITDQQGNV IAWASSGHVG
FKGSRKSTPF AAQLAAENAA RKAQEHGVRK VDVFVMGPGS GRETAIRSLQ AAGLEVGAIS
DVTPQPHNGC RPPKRRRV