ID   RS12_EIKCO              Reviewed;          98 AA.
AC   P35643;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=30S ribosomal protein S12;
DE   Flags: Fragment;
GN   Name=rpsL;
OS   Eikenella corrodens.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Eikenella.
OX   NCBI_TaxID=539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23834 / DSM 8340 / JCM 12952 / KCTC 15198 / LMG 15557 / NCTC
RC   10596 / 333/54-55;
RA   Rao V.K., Whitlock J.A., Progulske-Fox A.;
RL   Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the universal ribosomal protein uS12 family.
CC       {ECO:0000305}.
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DR   EMBL; Z12610; CAA78255.1; -; Genomic_DNA.
DR   PIR; S23849; S23849.
DR   AlphaFoldDB; P35643; -.
DR   SMR; P35643; -.
DR   STRING; 539.A7P85_03845; -.
DR   GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   CDD; cd03368; Ribosomal_S12; 1.
DR   Gene3D; 2.40.50.140; -; 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..98
FT                   /note="30S ribosomal protein S12"
FT                   /id="PRO_0000146222"
FT   REGION          79..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         64
FT                   /note="3-methylthioaspartic acid"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   98 AA;  10861 MW;  262161581F6359AE CRC64;
     ACPQKRGVCT RVYTTTPKKP NSALRKVCKV RLTNGFEVIS YIGGEGHNLQ EHSVVLIRGG
     RVKDLPGVRY HTVRGTLDTA GVKDRKQARS KYGAKRPK