RS12_HELPY
ID RS12_HELPY Reviewed; 135 AA.
AC P0A0X4; P56019; Q9R787;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=30S ribosomal protein S12;
GN Name=rpsL; OrderedLocusNames=HP_1197;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (OF A STREPTOMYCIN RESISTANT VARIANT).
RC STRAIN=DSM 4867 / CCUG 17874 / NCTC 11638;
RA Marchetti M., Censini S., Ghiara P., Rappuoli R., Covacci A.;
RT "Mutations affecting the colonizing-potential of Helicobacter pylori map
RT within the cag pathogenicity island.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=23093592; DOI=10.1093/nar/gks945;
RA Redko Y., Aubert S., Stachowicz A., Lenormand P., Namane A., Darfeuille F.,
RA Thibonnier M., De Reuse H.;
RT "A minimal bacterial RNase J-based degradosome is associated with
RT translating ribosomes.";
RL Nucleic Acids Res. 41:288-301(2013).
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 -!- INTERACTION:
CC P0A0X4; O25687: rimP; NbExp=3; IntAct=EBI-7607319, EBI-7605525;
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS12 family.
CC {ECO:0000305}.
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DR EMBL; AE000511; AAD08241.1; -; Genomic_DNA.
DR EMBL; U96106; AAD00825.1; -; Genomic_DNA.
DR PIR; E64669; E64669.
DR RefSeq; NP_207988.1; NC_000915.1.
DR RefSeq; WP_001142321.1; NC_018939.1.
DR AlphaFoldDB; P0A0X4; -.
DR SMR; P0A0X4; -.
DR IntAct; P0A0X4; 3.
DR MINT; P0A0X4; -.
DR STRING; 85962.C694_06190; -.
DR PaxDb; P0A0X4; -.
DR EnsemblBacteria; AAD08241; AAD08241; HP_1197.
DR GeneID; 66522383; -.
DR KEGG; hpy:HP_1197; -.
DR PATRIC; fig|85962.47.peg.1286; -.
DR eggNOG; COG0048; Bacteria.
DR OMA; SPALEKC; -.
DR PhylomeDB; P0A0X4; -.
DR Proteomes; UP000000429; 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:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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 Antibiotic resistance; Methylation; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding.
FT CHAIN 1..135
FT /note="30S ribosomal protein S12"
FT /id="PRO_0000146235"
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"
FT VARIANT 43
FT /note="K -> R (in strain: CCUG 17874; streptomycin
FT resistant)"
SQ SEQUENCE 135 AA; 15106 MW; 909C91470EB19959 CRC64;
MPTINQLIRK ERKKVVKKTK SPALVECPQR RGVCTRVYTT TPKKPNSALR KVAKVRLTSK
FEVISYIPGE GHNLQEHSIV LVRGGRVKDL PGVKYHIVRG ALDTAGVNKR TVSRSKYGTK
KAKATDKKAT DNKKK
