ID   RS12_LEPBI              Reviewed;         124 AA.
AC   P63198; P20820; P63197;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=30S ribosomal protein S12;
GN   Name=rpsL;
OS   Leptospira biflexa.
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=172;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Patoc I / Serovar Patoc;
RX   PubMed=2211535; DOI=10.1128/jb.172.10.6165-6168.1990;
RA   Zuerner R.L., Charon N.W.;
RT   "Nucleotide sequence analysis of the Leptospira biflexa serovar patoc rpsL
RT   and rpsG genes.";
RL   J. Bacteriol. 172:6165-6168(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Patoc I / Serovar patoc / PITAL;
RX   PubMed=11470352; DOI=10.1111/j.1574-6968.2001.tb10747.x;
RA   Brenot A., Werts C., Ottone C., Sertour N., Charon N.W., Postic D.,
RA   Baranton G., Saint Girons I.;
RT   "First evidence for a restriction-modification system in Leptospira sp.";
RL   FEMS Microbiol. Lett. 201:139-143(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   -!- SIMILARITY: Belongs to the universal ribosomal protein uS12 family.
CC       {ECO:0000305}.
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DR   EMBL; M57776; AAA63276.1; -; Genomic_DNA.
DR   EMBL; AJ310918; CAC44029.1; -; Genomic_DNA.
DR   RefSeq; WP_004783543.1; NZ_RQHE01000004.1.
DR   AlphaFoldDB; P63198; -.
DR   SMR; P63198; -.
DR   GeneID; 50044006; -.
DR   GeneID; 64279442; -.
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: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..124
FT                   /note="30S ribosomal protein S12"
FT                   /id="PRO_0000146248"
FT   MOD_RES         89
FT                   /note="3-methylthioaspartic acid"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   124 AA;  13948 MW;  F922286E5CC077C1 CRC64;
     MPTINQLIRI GREDQKKRTK SPALKACPQR RGVCTRVMTF TPKKPNSALR KVARVRLTTG
     IEVTAYIPGE GHNLQEHNVV LIRGGRVKDL PGVRYHIIRG TLDTLGVDKR RKGRSKYGAK
     RPKA