ID   RS12_RHOPA              Reviewed;         123 AA.
AC   Q6N4T2;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=30S ribosomal protein S12 {ECO:0000255|HAMAP-Rule:MF_00403};
DE   AltName: Full=RRP-S12;
GN   Name=rpsL {ECO:0000255|HAMAP-Rule:MF_00403}; OrderedLocusNames=RPA3255;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
RN   [2]
RP   METHYLTHIOLATION AT ASP-89, AND MASS SPECTROMETRY.
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=15473684; DOI=10.1021/pr049940z;
RA   Strader M.B., VerBerkmoes N.C., Tabb D.L., Connelly H.M., Barton J.W.,
RA   Bruce B.D., Pelletier D.A., Davison B.H., Hettich R.L., Larimer F.W.,
RA   Hurst G.B.;
RT   "Characterization of the 70S ribosome from Rhodopseudomonas palustris using
RT   an integrated 'top-down' and 'bottom-up' mass spectrometric approach.";
RL   J. Proteome Res. 3:965-978(2004).
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   -!- PTM: Both N-terminus methionine truncation and retention have been
CC       observed for this protein.
CC   -!- MASS SPECTROMETRY: Mass=13875.2; Method=Electrospray; Note=This is the
CC       mass for the protein without N-terminus methionine removal.;
CC       Evidence={ECO:0000269|PubMed:15473684};
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS12 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00403}.
CC   -!- CAUTION: Both N-terminus methionine truncation and retention have been
CC       observed for this protein by 2 different experiments. {ECO:0000305}.
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DR   EMBL; BX572603; CAE28696.1; -; Genomic_DNA.
DR   RefSeq; WP_008969396.1; NC_005296.1.
DR   AlphaFoldDB; Q6N4T2; -.
DR   SMR; Q6N4T2; -.
DR   IntAct; Q6N4T2; 1.
DR   STRING; 258594.RPA3255; -.
DR   PRIDE; Q6N4T2; -.
DR   EnsemblBacteria; CAE28696; CAE28696; RPA3255.
DR   GeneID; 66894341; -.
DR   KEGG; rpa:RPA3255; -.
DR   eggNOG; COG0048; Bacteria.
DR   HOGENOM; CLU_104295_1_2_5; -.
DR   OMA; SPALEKC; -.
DR   PhylomeDB; Q6N4T2; -.
DR   BioCyc; RPAL258594:TX73_RS16605-MON; -.
DR   Proteomes; UP000001426; 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   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   Methylation; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding; tRNA-binding.
FT   CHAIN           1..123
FT                   /note="30S ribosomal protein S12"
FT                   /id="PRO_0000146297"
FT   MOD_RES         89
FT                   /note="3-methylthioaspartic acid"
FT                   /evidence="ECO:0000269|PubMed:15473684"
SQ   SEQUENCE   123 AA;  13875 MW;  26E3A2843874F549 CRC64;
     MPTINQLIAN PRVVQKSRKK VPALQQSPQK RGVCTRVYTT TPKKPNSALR KVAKVRLTNG
     FEVIGYIPGE GHNLQEHSVV MIRGGRVKDL PGVRYHILRG VLDTQGVKNR KQRRSKYGAK
     RPK