RS12_STAA8
ID RS12_STAA8 Reviewed; 137 AA.
AC P0A0H0; P48942; Q2G0N3;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=30S ribosomal protein S12 {ECO:0000255|HAMAP-Rule:MF_00403};
GN Name=rpsL {ECO:0000255|HAMAP-Rule:MF_00403};
GN OrderedLocusNames=SAOUHSC_00527;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9573165; DOI=10.1128/jb.180.10.2759-2765.1998;
RA Wada A., Watanabe H.;
RT "Penicillin-binding protein 1 of Staphylococcus aureus is essential for
RT growth.";
RL J. Bacteriol. 180:2759-2765(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
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; U20869; AAC46353.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD29675.1; -; Genomic_DNA.
DR RefSeq; WP_001142337.1; NZ_LS483365.1.
DR RefSeq; YP_499099.1; NC_007795.1.
DR PDB; 5LI0; EM; 3.80 A; l=2-136.
DR PDB; 5ND8; EM; 3.70 A; l=1-137.
DR PDB; 5ND9; EM; 3.70 A; l=1-137.
DR PDB; 5TCU; EM; 3.90 A; S3=2-137.
DR PDB; 6YEF; EM; 3.20 A; l=1-137.
DR PDB; 7BGD; EM; 3.20 A; l=1-137.
DR PDB; 7KWG; EM; 3.75 A; l=1-137.
DR PDB; 7NHL; EM; 3.10 A; m=1-137.
DR PDB; 7NHM; EM; 3.10 A; m=1-137.
DR PDBsum; 5LI0; -.
DR PDBsum; 5ND8; -.
DR PDBsum; 5ND9; -.
DR PDBsum; 5TCU; -.
DR PDBsum; 6YEF; -.
DR PDBsum; 7BGD; -.
DR PDBsum; 7KWG; -.
DR PDBsum; 7NHL; -.
DR PDBsum; 7NHM; -.
DR AlphaFoldDB; P0A0H0; -.
DR SMR; P0A0H0; -.
DR IntAct; P0A0H0; 1.
DR STRING; 1280.SAXN108_0599; -.
DR EnsemblBacteria; ABD29675; ABD29675; SAOUHSC_00527.
DR GeneID; 3920380; -.
DR GeneID; 66838837; -.
DR KEGG; sao:SAOUHSC_00527; -.
DR PATRIC; fig|93061.5.peg.473; -.
DR eggNOG; COG0048; Bacteria.
DR HOGENOM; CLU_104295_1_2_9; -.
DR OMA; SPALEKC; -.
DR PRO; PR:P0A0H0; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005840; C:ribosome; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Methylation; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding.
FT CHAIN 1..137
FT /note="30S ribosomal protein S12"
FT /id="PRO_0000146312"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 102
FT /note="3-methylthioaspartic acid"
FT /evidence="ECO:0000250"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:7BGD"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:7BGD"
FT TURN 30..33
FT /evidence="ECO:0007829|PDB:7BGD"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:7BGD"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:7BGD"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:7BGD"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:7BGD"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:7BGD"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:7BGD"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:7BGD"
FT TURN 128..131
FT /evidence="ECO:0007829|PDB:7BGD"
SQ SEQUENCE 137 AA; 15287 MW; 5E973910C6F97995 CRC64;
MPTINQLVRK PRQSKIKKSD SPALNKGFNS KKKKFTDLNS PQKRGVCTRV GTMTPKKPNS
ALRKYARVRL SNNIEINAYI PGIGHNLQEH SVVLVRGGRV KDLPGVRYHI VRGALDTSGV
DGRRQGRSLY GTKKPKN