ID   RS12_STRLI              Reviewed;         123 AA.
AC   P0A4A5; P97222;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=30S ribosomal protein S12;
GN   Name=rpsL;
OS   Streptomyces lividans.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND STREPTOMYCIN RESISTANT VARIANTS.
RC   STRAIN=TK21;
RX   PubMed=8955413; DOI=10.1128/jb.178.24.7276-7284.1996;
RA   Shima J., Hesketh A., Okamoto S., Kawamoto S., Ochi K.;
RT   "Induction of actinorhodin production by rpsL (encoding ribosomal protein
RT   S12) mutations that confer streptomycin resistance in Streptomyces lividans
RT   and Streptomyces coelicolor A3(2).";
RL   J. Bacteriol. 178:7276-7284(1996).
CC   -!- FUNCTION: With S4 and S5 plays an important role in translational
CC       accuracy. {ECO:0000250}.
CC   -!- FUNCTION: Interacts with and stabilizes bases of the 16S rRNA that are
CC       involved in tRNA selection in the A site and with the mRNA backbone.
CC       Located at the interface of the 30S and 50S subunits, it traverses the
CC       body of the 30S subunit contacting proteins on the other side and
CC       probably holding the rRNA structure together. The combined cluster of
CC       proteins S8, S12 and S17 appears to hold together the shoulder and
CC       platform of the 30S subunit (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S8 and
CC       S17. May interact with IF1 in the 30S initiation complex (By
CC       similarity). {ECO:0000250}.
CC   -!- BIOTECHNOLOGY: One streptomycin resistant strain of S.coelicolor and
CC       S.lividans (K88E) produces increased quantities of the natural
CC       antibiotic actinorhodin; strains which are resistant to multiple drugs
CC       produce more antibiotic.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS12 family.
CC       {ECO:0000305}.
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DR   EMBL; D83746; BAA12096.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0A4A5; -.
DR   SMR; P0A4A5; -.
DR   GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd03368; Ribosomal_S12; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   HAMAP; MF_00403_B; Ribosomal_S12_B; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR006032; Ribosomal_S12/S23.
DR   InterPro; IPR005679; Ribosomal_S12_bac.
DR   PANTHER; PTHR11652; PTHR11652; 1.
DR   Pfam; PF00164; Ribosom_S12_S23; 1.
DR   PIRSF; PIRSF002133; Ribosomal_S12/S23; 1.
DR   PRINTS; PR01034; RIBOSOMALS12.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00981; rpsL_bact; 1.
DR   PROSITE; PS00055; RIBOSOMAL_S12; 1.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; Methylation; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding; tRNA-binding.
FT   CHAIN           1..123
FT                   /note="30S ribosomal protein S12"
FT                   /id="PRO_0000146323"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         89
FT                   /note="3-methylthioaspartic acid"
FT                   /evidence="ECO:0000250"
FT   VARIANT         88
FT                   /note="K -> E (streptomycin resistant mutant. Increases
FT                   antibiotic production)"
SQ   SEQUENCE   123 AA;  13771 MW;  9F9C1621AD40D5A0 CRC64;
     MPTIQQLVRK GRQDKVEKNK TPALEGSPQR RGVCTRVFTT TPKKPNSALR KVARVRLTSG
     IEVTAYIPGE GHNLQEHSIV LVRGGRVKDL PGVRYKIIRG SLDTQGVKNR KQARSRYGAK
     KEK