RS12_THET2
ID RS12_THET2 Reviewed; 132 AA.
AC P61941;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=30S ribosomal protein S12;
GN Name=rpsL; Synonyms=rps12; OrderedLocusNames=TT_C1333;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS81675.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE017221; AAS81675.1; ALT_INIT; Genomic_DNA.
DR PDB; 2R1G; EM; -; H=2-125.
DR PDB; 4KVB; X-ray; 4.20 A; L=1-132.
DR PDB; 4V4I; X-ray; 3.71 A; m=1-132.
DR PDB; 4V4J; X-ray; 3.83 A; m=1-132.
DR PDB; 4V63; X-ray; 3.21 A; AL/CL=1-132.
DR PDB; 4V67; X-ray; 3.00 A; AL/CL=1-132.
DR PDB; 4V7P; X-ray; 3.62 A; AL/DL=2-125.
DR PDB; 4V83; X-ray; 3.50 A; AL/CL=2-125.
DR PDB; 4V84; X-ray; 3.40 A; AL/CL=2-125.
DR PDB; 4V9J; X-ray; 3.86 A; AL/CL=2-126.
DR PDB; 4V9K; X-ray; 3.50 A; AL/CL=2-126.
DR PDB; 4V9L; X-ray; 3.50 A; AL/CL=2-126.
DR PDB; 4V9M; X-ray; 4.00 A; AL/CL=2-126.
DR PDB; 4V9N; X-ray; 3.40 A; AL/CL=2-123.
DR PDB; 4V9Q; X-ray; 3.40 A; BL/DL=2-123.
DR PDB; 4W29; X-ray; 3.80 A; AL/CL=2-126.
DR PDB; 4XEJ; X-ray; 3.80 A; AS12/BS12=2-123.
DR PDB; 5J4D; X-ray; 3.10 A; UA/ZC=1-132.
DR PDBsum; 2R1G; -.
DR PDBsum; 4KVB; -.
DR PDBsum; 4V4I; -.
DR PDBsum; 4V4J; -.
DR PDBsum; 4V63; -.
DR PDBsum; 4V67; -.
DR PDBsum; 4V7P; -.
DR PDBsum; 4V83; -.
DR PDBsum; 4V84; -.
DR PDBsum; 4V9J; -.
DR PDBsum; 4V9K; -.
DR PDBsum; 4V9L; -.
DR PDBsum; 4V9M; -.
DR PDBsum; 4V9N; -.
DR PDBsum; 4V9Q; -.
DR PDBsum; 4W29; -.
DR PDBsum; 4XEJ; -.
DR PDBsum; 5J4D; -.
DR AlphaFoldDB; P61941; -.
DR SMR; P61941; -.
DR IntAct; P61941; 4.
DR STRING; 262724.TT_C1333; -.
DR EnsemblBacteria; AAS81675; AAS81675; TT_C1333.
DR KEGG; tth:TT_C1333; -.
DR eggNOG; COG0048; Bacteria.
DR HOGENOM; CLU_104295_1_2_0; -.
DR OMA; SPALEKC; -.
DR EvolutionaryTrace; P61941; -.
DR Proteomes; UP000000592; 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 1: Evidence at protein level;
KW 3D-structure; Methylation; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..132
FT /note="30S ribosomal protein S12"
FT /id="PRO_0000146340"
FT REGION 106..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 89
FT /note="3-methylthioaspartic acid"
FT /evidence="ECO:0000250"
FT HELIX 4..8
FT /evidence="ECO:0007829|PDB:4V67"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:4V63"
FT STRAND 30..40
FT /evidence="ECO:0007829|PDB:4V67"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:4V84"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4V63"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:4V9L"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:4V67"
SQ SEQUENCE 132 AA; 14599 MW; 9943D095FAD4D9BC CRC64;
MPTINQLVRK GREKVRKKSK VPALKGAPFR RGVCTVVRTV TPKKPNSALR KVAKVRLTSG
YEVTAYIPGE GHNLQEHSVV LIRGGRVKDL PGVRYHIVRG VYDAAGVKDR KKSRSKYGTK
KPKEAAKTAA KK
