(data stored in ACNUC7421 zone)

SWISSPROT: RS12_POLNA

ID   RS12_POLNA              Reviewed;         125 AA.
AC   A1VIP5;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   11-DEC-2019, entry version 70.
DE   RecName: Full=30S ribosomal protein S12 {ECO:0000255|HAMAP-Rule:MF_00403};
GN   Name=rpsL {ECO:0000255|HAMAP-Rule:MF_00403}; OrderedLocusNames=Pnap_0198;
OS   Polaromonas naphthalenivorans (strain CJ2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=365044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ2;
RX   PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA   Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT   "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT   tar-contaminated sediment, reveals physiological and metabolic versatility
RT   and evolution through extensive horizontal gene transfer.";
RL   Environ. Microbiol. 11:2253-2270(2009).
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}.
DR   EMBL; CP000529; ABM35523.1; -; Genomic_DNA.
DR   RefSeq; WP_011799633.1; NC_008781.1.
DR   SMR; A1VIP5; -.
DR   STRING; 365044.Pnap_0198; -.
DR   EnsemblBacteria; ABM35523; ABM35523; Pnap_0198.
DR   KEGG; pna:Pnap_0198; -.
DR   eggNOG; ENOG4108UKE; Bacteria.
DR   eggNOG; COG0048; LUCA.
DR   HOGENOM; HOG000040063; -.
DR   KO; K02950; -.
DR   OMA; SPALEKC; -.
DR   OrthoDB; 1707228at2; -.
DR   Proteomes; UP000000644; 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:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd03368; Ribosomal_S12; 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;
DR   PRODOM; A1VIP5.
DR   SWISS-2DPAGE; A1VIP5.
KW   Methylation; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding; tRNA-binding.
FT   CHAIN           1..125
FT                   /note="30S ribosomal protein S12"
FT                   /id="PRO_0000296012"
FT   MOD_RES         89
FT                   /note="3-methylthioaspartic acid"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   125 AA;  14018 MW;  1825FCDD5AA6FE07 CRC64;
     MPTINQLVRQ GREVEKIKSK SPAMENSPQR RGVCTRVYTT TPKKPNSALR KVAKVRLTNG
     FEIISYIGGE GHNLQEHSVV LVRGGRVKDL PGVRYHIVRG SLDLQGVKDR KQSRSKYGAK
     RPKAK
//

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