GenomeNet

Database: UniProt
Entry: B1JU17
LinkDB: B1JU17
Original site: B1JU17 
ID   RS12_BURO0              Reviewed;         126 AA.
AC   B1JU17;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=Small ribosomal subunit protein uS12 {ECO:0000255|HAMAP-Rule:MF_00403};
DE   AltName: Full=30S ribosomal protein S12 {ECO:0000305};
GN   Name=rpsL {ECO:0000255|HAMAP-Rule:MF_00403};
GN   OrderedLocusNames=Bcenmc03_0322;
OS   Burkholderia orbicola (strain MC0-3).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex;
OC   Burkholderia orbicola.
OX   NCBI_TaxID=406425;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC0-3;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA   Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cenocepacia MC0-3.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000958; ACA89502.1; -; Genomic_DNA.
DR   RefSeq; WP_006400662.1; NC_010508.1.
DR   AlphaFoldDB; B1JU17; -.
DR   SMR; B1JU17; -.
DR   GeneID; 84791211; -.
DR   KEGG; bcm:Bcenmc03_0322; -.
DR   HOGENOM; CLU_104295_1_2_4; -.
DR   Proteomes; UP000002169; Chromosome 1.
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: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   3: Inferred from homology;
KW   Methylation; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding; tRNA-binding.
FT   CHAIN           1..126
FT                   /note="Small ribosomal subunit protein uS12"
FT                   /id="PRO_1000194136"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          103..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         89
FT                   /note="3-methylthioaspartic acid"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   126 AA;  13999 MW;  7C8DEA67315E816C CRC64;
     MPTINQLVRK GRQSETTKSK SPALQDCPQR RGVCTRVYTT TPKKPNSALR KVAKVRLTNG
     FEVISYIGGE GHNLQEHSVV LIRGGRVKDL PGVRYHMVRG SLDTQGVKDR KQARSKYGAK
     RAKAAK
//
DBGET integrated database retrieval system