RS12_THETH
ID RS12_THETH Reviewed; 132 AA.
AC P17293; Q9EYQ6;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 148.
DE RecName: Full=30S ribosomal protein S12;
GN Name=rpsL; Synonyms=rps12;
OS Thermus thermophilus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=274;
RN [1]
RP PROTEIN SEQUENCE OF 2-8.
RC STRAIN=VK1;
RX PubMed=1637860; DOI=10.1016/0300-9084(92)90110-z;
RA Garber M.B., Agalarov S.C., Eliseikina I.A., Fomenkova N.P., Nikonov S.V.,
RA Sedelnikova S.E., Shikaeva O.S., Vasiliev D., Zhdanov A.S., Liljas A.,
RA Svensson L.A.;
RT "Ribosomal proteins from Thermus thermophilus for structural
RT investigations.";
RL Biochimie 74:327-336(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-132, AND STREPTOMYCIN RESISTANT
RP VARIANTS.
RC STRAIN=ATCC 43815 / IB-21;
RX PubMed=11371156; DOI=10.1006/jmbi.2001.4676;
RA Gregory S.T., Cate J.H.D., Dahlberg A.E.;
RT "Streptomycin-resistant and streptomycin-dependent mutants of the extreme
RT thermophile Thermus thermophilus.";
RL J. Mol. Biol. 309:333-338(2001).
RN [3]
RP MASS SPECTROMETRY, AND METHYLTHIOLATION AT ASP-89.
RC STRAIN=ATCC 43815 / IB-21;
RX PubMed=16287167; DOI=10.1002/pmic.200402111;
RA Suh M.-J., Hamburg D.M., Gregory S.T., Dahlberg A.E., Limbach P.A.;
RT "Extending ribosomal protein identifications to unsequenced bacterial
RT strains using matrix-assisted laser desorption/ionization mass
RT spectrometry.";
RL Proteomics 5:4818-4831(2005).
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 -!- MASS SPECTROMETRY: Mass=14516; Method=MALDI; Note=Strain IB-21.;
CC Evidence={ECO:0000269|PubMed:16287167};
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS12 family.
CC {ECO:0000305}.
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DR EMBL; AF316617; AAG38586.1; -; Genomic_DNA.
DR PDB; 2OM7; EM; 7.30 A; E=1-132.
DR PDB; 4V8X; X-ray; 3.35 A; AL/CL=1-132.
DR PDBsum; 2OM7; -.
DR PDBsum; 4V8X; -.
DR AlphaFoldDB; P17293; -.
DR SMR; P17293; -.
DR IntAct; P17293; 1.
DR MINT; P17293; -.
DR EvolutionaryTrace; P17293; -.
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:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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; Antibiotic resistance; Direct protein sequencing;
KW Methylation; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding; tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1637860"
FT CHAIN 2..132
FT /note="30S ribosomal protein S12"
FT /id="PRO_0000146342"
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:0000269|PubMed:16287167"
FT VARIANT 42
FT /note="P -> S (in strain: Isolate HG18; streptomycin
FT resistant)"
FT VARIANT 43
FT /note="K -> R (in strain: Isolate HG3; streptomycin
FT resistant)"
FT VARIANT 86
FT /note="R -> C (in strain: Isolate HG14; streptomycin
FT pseudo-dependent)"
FT VARIANT 86
FT /note="R -> H (in strain: Isolate HG31; streptomycin
FT pseudo-dependent)"
FT VARIANT 88
FT /note="K -> E (in strain: Isolate HG19; streptomycin
FT resistant)"
FT VARIANT 88
FT /note="K -> R (in strain: Isolate HG1; streptomycin
FT resistant)"
FT VARIANT 91
FT /note="P -> L (in strain: Isolate HG11; streptomycin
FT dependent)"
FT HELIX 4..9
FT /evidence="ECO:0007829|PDB:4V8X"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:4V8X"
FT STRAND 30..40
FT /evidence="ECO:0007829|PDB:4V8X"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:4V8X"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:4V8X"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:4V8X"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:4V8X"
SQ SEQUENCE 132 AA; 14599 MW; 9943D095FAD4D9BC CRC64;
MPTINQLVRK GREKVRKKSK VPALKGAPFR RGVCTVVRTV TPKKPNSALR KVAKVRLTSG
YEVTAYIPGE GHNLQEHSVV LIRGGRVKDL PGVRYHIVRG VYDAAGVKDR KKSRSKYGTK
KPKEAAKTAA KK
