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RS12_LYSSC
ID   RS12_LYSSC              Reviewed;         139 AA.
AC   B1HMZ3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=30S ribosomal protein S12 {ECO:0000255|HAMAP-Rule:MF_00403};
GN   Name=rpsL {ECO:0000255|HAMAP-Rule:MF_00403}; OrderedLocusNames=Bsph_4627;
OS   Lysinibacillus sphaericus (strain C3-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=444177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C3-41;
RX   PubMed=18296527; DOI=10.1128/jb.01652-07;
RA   Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA   Berry C., Yuan Z.;
RT   "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT   sphaericus C3-41 and comparison with those of closely related Bacillus
RT   species.";
RL   J. Bacteriol. 190:2892-2902(2008).
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; CP000817; ACA42071.1; -; Genomic_DNA.
DR   RefSeq; WP_010860613.1; NC_010382.1.
DR   AlphaFoldDB; B1HMZ3; -.
DR   SMR; B1HMZ3; -.
DR   EnsemblBacteria; ACA42071; ACA42071; Bsph_4627.
DR   GeneID; 48274774; -.
DR   KEGG; lsp:Bsph_4627; -.
DR   HOGENOM; CLU_104295_1_2_9; -.
DR   OMA; SPALEKC; -.
DR   Proteomes; UP000002164; 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   Methylation; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding; tRNA-binding.
FT   CHAIN           1..139
FT                   /note="30S ribosomal protein S12"
FT                   /id="PRO_1000194188"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         102
FT                   /note="3-methylthioaspartic acid"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   139 AA;  15550 MW;  C0FA5E4889644604 CRC64;
     MPTINQLVRK PRQSKITKSK SPALNKGYNS FKKSLTDVKS PQKRGVCTRV GTMTPRKPNS
     ALRKYARVRL TNQIEVTAYI PGEGHNLQEH SVVLIRGGRV KDLAGVRYHI VRGALDTAGV
     NGRLQSRSKY GTKRPKEKK
 
 
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