RS12_AQUAE
ID RS12_AQUAE Reviewed; 128 AA.
AC O70089;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=30S ribosomal protein S12 {ECO:0000255|HAMAP-Rule:MF_00403};
GN Name=rpsL1 {ECO:0000255|HAMAP-Rule:MF_00403}; OrderedLocusNames=aq_1834;
GN and
GN Name=rpsL2 {ECO:0000255|HAMAP-Rule:MF_00403}; OrderedLocusNames=aq_735;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- FUNCTION: With S4 and S5 plays an important role in translational
CC accuracy. {ECO:0000255|HAMAP-Rule:MF_00403}.
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. {ECO:0000255|HAMAP-Rule:MF_00403}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S8 and
CC S17. May interact with IF1 in the 30S initiation complex.
CC {ECO:0000255|HAMAP-Rule:MF_00403}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS12 family.
CC {ECO:0000255|HAMAP-Rule:MF_00403}.
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; AE000657; AAC07655.1; -; Genomic_DNA.
DR EMBL; AE000657; AAC06910.1; -; Genomic_DNA.
DR PIR; H70457; H70457.
DR RefSeq; NP_213505.1; NC_000918.1.
DR RefSeq; NP_214257.1; NC_000918.1.
DR RefSeq; WP_010880443.1; NC_000918.1.
DR AlphaFoldDB; O70089; -.
DR SMR; O70089; -.
DR STRING; 224324.aq_1834; -.
DR EnsemblBacteria; AAC06910; AAC06910; aq_735.
DR EnsemblBacteria; AAC07655; AAC07655; aq_1834.
DR KEGG; aae:aq_1834; -.
DR KEGG; aae:aq_735; -.
DR PATRIC; fig|224324.8.peg.1415; -.
DR eggNOG; COG0048; Bacteria.
DR HOGENOM; CLU_104295_1_2_0; -.
DR InParanoid; O70089; -.
DR OMA; SPALEKC; -.
DR OrthoDB; 1707228at2; -.
DR Proteomes; UP000000798; 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: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 3: Inferred from homology;
KW Methylation; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; tRNA-binding.
FT CHAIN 1..128
FT /note="30S ribosomal protein S12"
FT /id="PRO_0000146166"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..128
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 128 AA; 14207 MW; 64731C4F359ECCD9 CRC64;
MPTFNQLVKY GREKRKKKSK APALQGCPQK RGVCVRVYTV TPKKPNSALR KVARVRLSNG
IEVTAYIPGE GHNLQEHSIV LVRGGRVKDL PGVRYKIIRG ALDAAGVEGR RQSRSKYGTK
RPKEEKGG
