RS12_HELPJ
ID RS12_HELPJ Reviewed; 135 AA.
AC P0A0X5; P56019; Q9R787;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=30S ribosomal protein S12;
GN Name=rpsL; OrderedLocusNames=jhp_1120;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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}.
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DR EMBL; AE001439; AAD06691.1; -; Genomic_DNA.
DR PIR; E64669; E64669.
DR RefSeq; WP_001142321.1; NZ_CP011330.1.
DR AlphaFoldDB; P0A0X5; -.
DR SMR; P0A0X5; -.
DR STRING; 85963.jhp_1120; -.
DR EnsemblBacteria; AAD06691; AAD06691; jhp_1120.
DR GeneID; 66522383; -.
DR KEGG; hpj:jhp_1120; -.
DR PATRIC; fig|85963.30.peg.1457; -.
DR eggNOG; COG0048; Bacteria.
DR OMA; SPALEKC; -.
DR Proteomes; UP000000804; 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: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 3: Inferred from homology;
KW Antibiotic resistance; Methylation; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; tRNA-binding.
FT CHAIN 1..135
FT /note="30S ribosomal protein S12"
FT /id="PRO_0000146236"
FT REGION 108..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 89
FT /note="3-methylthioaspartic acid"
FT /evidence="ECO:0000250"
SQ SEQUENCE 135 AA; 15106 MW; 909C91470EB19959 CRC64;
MPTINQLIRK ERKKVVKKTK SPALVECPQR RGVCTRVYTT TPKKPNSALR KVAKVRLTSK
FEVISYIPGE GHNLQEHSIV LVRGGRVKDL PGVKYHIVRG ALDTAGVNKR TVSRSKYGTK
KAKATDKKAT DNKKK