RS12_MYCSM
ID RS12_MYCSM Reviewed; 124 AA.
AC P0C563; P41195;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=30S ribosomal protein S12;
GN Name=rpsL;
OS Mycolicibacterium smegmatis (Mycobacterium smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1772;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS STREPTOMYCIN RESISTANT, AND
RP DOMINANCE OF THE STREPTOMYCIN SENSITIVE ALLELE.
RC STRAIN=LR222;
RX PubMed=7928982; DOI=10.1128/jb.176.19.6153-6156.1994;
RA Kenney T.J., Churchward G.;
RT "Cloning and sequence analysis of the rpsL and rpsG genes of Mycobacterium
RT smegmatis and characterization of mutations causing resistance to
RT streptomycin.";
RL J. Bacteriol. 176:6153-6156(1994).
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 -!- MISCELLANEOUS: The streptomycin sensitive allele is dominant to the
CC resistant allele in M.smegmatis.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS12 family.
CC {ECO:0000305}.
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DR EMBL; L34681; AAA62390.1; -; Genomic_DNA.
DR RefSeq; WP_007167812.1; NZ_UGQO01000001.1.
DR AlphaFoldDB; P0C563; -.
DR SMR; P0C563; -.
DR STRING; 710686.Mycsm_00973; -.
DR GeneID; 66732857; -.
DR eggNOG; COG0048; Bacteria.
DR OMA; SPALEKC; -.
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 3: Inferred from homology;
KW Antibiotic resistance; Methylation; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; tRNA-binding.
FT CHAIN 1..124
FT /note="30S ribosomal protein S12"
FT /id="PRO_0000146270"
FT REGION 105..124
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 (streptomycin resistant)"
FT VARIANT 43
FT /note="K -> R (streptomycin resistant)"
FT VARIANT 43
FT /note="K -> T (streptomycin resistant)"
FT VARIANT 86
FT /note="R -> L (streptomycin resistant)"
FT VARIANT 88
FT /note="K -> E (streptomycin resistant)"
FT VARIANT 88
FT /note="K -> R (streptomycin resistant)"
FT VARIANT 91
FT /note="P -> H (streptomycin resistant)"
SQ SEQUENCE 124 AA; 13863 MW; 669BE4F3AD829616 CRC64;
MPTIQQLVRK GRRDKIAKVK TAALKGSPQR RGVCTRVYTT TPKKPNSALR KVARVKLTSQ
VEVTAYIPGE GHNLQEHSMV LVRGGRVKDL PGVRYKIIRG SLDTQGVKNR KQARSRYGAK
KEKS