ID   RS12_TREPR              Reviewed;         126 AA.
AC   Q8KTP6;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=30S ribosomal protein S12 {ECO:0000255|HAMAP-Rule:MF_00403};
GN   Name=rpsL {ECO:0000255|HAMAP-Rule:MF_00403};
GN   Synonyms=rps12 {ECO:0000255|HAMAP-Rule:MF_00403};
OS   Tremblaya princeps.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Candidatus Tremblaya.
OX   NCBI_TaxID=189385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12088995; DOI=10.1128/aem.68.7.3198-3205.2002;
RA   Baumann L., Thao M.L., Hess J.M., Johnson M.W., Baumann P.;
RT   "The genetic properties of the primary endosymbionts of mealybugs differ
RT   from those of other endosymbionts of plant sap-sucking insects.";
RL   Appl. Environ. Microbiol. 68:3198-3205(2002).
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}.
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DR   EMBL; AF481103; AAM76002.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8KTP6; -.
DR   SMR; Q8KTP6; -.
DR   STRING; 1053648.TCP_116; -.
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   Methylation; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding; tRNA-binding.
FT   CHAIN           1..126
FT                   /note="30S ribosomal protein S12"
FT                   /id="PRO_0000146200"
FT   REGION          106..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         89
FT                   /note="3-methylthioaspartic acid"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   126 AA;  14075 MW;  99089A35B6D2CA4B CRC64;
     MPTLNQLVRQ GRRRFEARSK SPALRGCPQL RGVCTKVYTT TPKKPNSALR KVAKVRLSNR
     LEVISYIGGE GHNLQEHSMV LVRGGRVKDL PGVRYHIVRG ALDAGGVRER RRSRSKYGAK
     MPRSAA