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RS12_STRPN
ID   RS12_STRPN              Reviewed;         137 AA.
AC   P0A4A7; P30891;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=30S ribosomal protein S12 {ECO:0000255|HAMAP-Rule:MF_00403};
GN   Name=rpsL {ECO:0000255|HAMAP-Rule:MF_00403}; Synonyms=str;
GN   OrderedLocusNames=SP_0271;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=R6 / R800;
RX   PubMed=1461744; DOI=10.1093/nar/20.22.6103;
RA   Salles C., Creancier L., Claverys J.-P., Mejean V.;
RT   "The high level streptomycin resistance gene from Streptococcus pneumoniae
RT   is a homologue of the ribosomal protein S12 gene from Escherichia coli.";
RL   Nucleic Acids Res. 20:6103-6103(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
CC   -!- FUNCTION: With S4 and S5 plays an important role in translational
CC       accuracy. {ECO:0000255|HAMAP-Rule:MF_00403}.
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. {ECO:0000255|HAMAP-Rule:MF_00403}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S8 and
CC       S17. May interact with IF1 in the 30S initiation complex.
CC       {ECO:0000255|HAMAP-Rule:MF_00403}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS12 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00403}.
CC   -!- CAUTION: Because the enzyme that would modify Asp-102 to 3-
CC       methylthioaspartic acid has not been found in the proteome of this
CC       organism, that modification is not predicted. {ECO:0000305}.
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DR   EMBL; Z15120; CAA78825.1; -; Genomic_DNA.
DR   EMBL; AE005672; AAK74449.1; -; Genomic_DNA.
DR   PIR; H95031; H95031.
DR   PIR; S26680; S26680.
DR   RefSeq; WP_001142332.1; NZ_AKVY01000001.1.
DR   AlphaFoldDB; P0A4A7; -.
DR   SMR; P0A4A7; -.
DR   STRING; 170187.SP_0271; -.
DR   EnsemblBacteria; AAK74449; AAK74449; SP_0271.
DR   GeneID; 60232916; -.
DR   GeneID; 64075287; -.
DR   KEGG; spn:SP_0271; -.
DR   eggNOG; COG0048; Bacteria.
DR   OMA; SPALEKC; -.
DR   PhylomeDB; P0A4A7; -.
DR   BioCyc; SPNE170187:G1FZB-277-MON; -.
DR   Proteomes; UP000000585; Chromosome.
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: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   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW   tRNA-binding.
FT   CHAIN           1..137
FT                   /note="30S ribosomal protein S12"
FT                   /id="PRO_0000146325"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         56
FT                   /note="K -> T (in STR41 mutation, high level of resistance
FT                   to streptomycin)"
SQ   SEQUENCE   137 AA;  15144 MW;  4BD0EF63BDFE4FFA CRC64;
     MPTINQLVRK PRKSKVEKSK SPALNVGYNS HKKVQTNVSS PQKRGVATRV GTMTPKKPNS
     ALRKFARVRL SNLIEVTAYI PGIGHNLQEH SVVLLRGGRV KDLPGVRYHI VRGALDTAGV
     NDRKQGRSKY GTKRPKA
 
 
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