RS12_STRCO
ID RS12_STRCO Reviewed; 123 AA.
AC P0A4A3; P97222;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=30S ribosomal protein S12;
GN Name=rpsL; OrderedLocusNames=SCO4659; ORFNames=SCD40A.05;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS STREPTOMYCIN RESISTANT.
RC STRAIN=A3(2) / 1147;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [3]
RP VARIANT STREPTOMYCIN RESISTANT, AND ANTIBIOTIC PRODUCTION.
RC STRAIN=A3(2) / 1147;
RX PubMed=11282646; DOI=10.1128/aem.67.4.1885-1892.2001;
RA Hu H., Ochi K.;
RT "Novel approach for improving the productivity of antibiotic-producing
RT strains by inducing combined resistant mutations.";
RL Appl. Environ. Microbiol. 67:1885-1892(2001).
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; AL939121; CAB81850.1; -; Genomic_DNA.
DR RefSeq; NP_628819.1; NC_003888.3.
DR RefSeq; WP_003948652.1; NZ_VNID01000028.1.
DR AlphaFoldDB; P0A4A3; -.
DR SMR; P0A4A3; -.
DR STRING; 100226.SCO4659; -.
DR ChEMBL; CHEMBL1641336; -.
DR GeneID; 1100100; -.
DR GeneID; 58470329; -.
DR GeneID; 63982115; -.
DR GeneID; 67401280; -.
DR KEGG; sco:SCO4659; -.
DR PATRIC; fig|100226.15.peg.4730; -.
DR eggNOG; COG0048; Bacteria.
DR HOGENOM; CLU_104295_1_2_11; -.
DR InParanoid; P0A4A3; -.
DR OMA; SPALEKC; -.
DR PhylomeDB; P0A4A3; -.
DR PRO; PR:P0A4A3; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005840; C:ribosome; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
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; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding.
FT CHAIN 1..123
FT /note="30S ribosomal protein S12"
FT /id="PRO_0000146320"
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 43
FT /note="K -> N (in strain: STRA1; streptomycin resistant
FT mutant which does not increase antibiotic production)"
FT VARIANT 86
FT /note="R -> H (in strain: KO-150 and KO-151; low level
FT streptomycin resistant mutants which increase antibiotic
FT production)"
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
