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 27-MAR-2024, entry version 155. DE RecName: Full=Small ribosomal subunit protein uS12 {ECO:0000305}; DE AltName: Full=30S ribosomal protein S12; GN Name=rpsL; Synonyms=rps12; OS Thermus thermophilus. OC Bacteria; Deinococcota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 OMA; MHRQGPP; -. 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; Nucleic acid-binding proteins; 1. DR HAMAP; MF_00403_B; Ribosomal_uS12_B; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR006032; Ribosomal_uS12. DR InterPro; IPR005679; Ribosomal_uS12_bac. DR NCBIfam; TIGR00981; rpsL_bact; 1. DR PANTHER; PTHR11652:SF1; 28S RIBOSOMAL PROTEIN S12, MITOCHONDRIAL; 1. DR PANTHER; PTHR11652; 30S RIBOSOMAL PROTEIN S12 FAMILY MEMBER; 1. DR Pfam; PF00164; Ribosom_S12_S23; 1. DR PIRSF; PIRSF002133; Ribosomal_S12/S23; 1. DR PRINTS; PR01034; RIBOSOMALS12. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 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="Small ribosomal subunit protein uS12" 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 //