RS12_MACCJ
ID RS12_MACCJ Reviewed; 139 AA.
AC B9E8Q3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=30S ribosomal protein S12 {ECO:0000255|HAMAP-Rule:MF_00403};
GN Name=rpsL {ECO:0000255|HAMAP-Rule:MF_00403}; OrderedLocusNames=MCCL_1864;
OS Macrococcus caseolyticus (strain JCSC5402).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; Macrococcus.
OX NCBI_TaxID=458233;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC5402;
RX PubMed=19074389; DOI=10.1128/jb.01058-08;
RA Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.;
RT "Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402,
RT reflecting the ancestral genome of the human-pathogenic staphylococci.";
RL J. Bacteriol. 191:1180-1190(2009).
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; AP009484; BAH18571.1; -; Genomic_DNA.
DR RefSeq; WP_015912363.1; NC_011999.1.
DR AlphaFoldDB; B9E8Q3; -.
DR SMR; B9E8Q3; -.
DR STRING; 458233.MCCL_1864; -.
DR EnsemblBacteria; BAH18571; BAH18571; MCCL_1864.
DR GeneID; 61130249; -.
DR GeneID; 66512913; -.
DR KEGG; mcl:MCCL_1864; -.
DR eggNOG; COG0048; Bacteria.
DR HOGENOM; CLU_104295_1_2_9; -.
DR OMA; SPALEKC; -.
DR OrthoDB; 1707228at2; -.
DR Proteomes; UP000001383; 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 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; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; tRNA-binding.
FT CHAIN 1..139
FT /note="30S ribosomal protein S12"
FT /id="PRO_1000134641"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 102
FT /note="3-methylthioaspartic acid"
FT /evidence="ECO:0000250"
SQ SEQUENCE 139 AA; 15310 MW; 1F67A479D5260FAA CRC64;
MPTINQLVKK PRTSKVKKST APALNKGYNS HKKKATDLAS PQKRGVCTRV GTMTPKKPNS
ALRKYARVRL SNNIEVNAYI PGIGHNLQEH SVVLIRGGRV KDLPGVRYHI VRGALDTSGV
DGRMQGRSLY GAKKPKEKK