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RS12_ENTFA
ID   RS12_ENTFA              Reviewed;         137 AA.
AC   Q839H1;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=30S ribosomal protein S12 {ECO:0000255|HAMAP-Rule:MF_00403};
GN   Name=rpsL {ECO:0000255|HAMAP-Rule:MF_00403}; OrderedLocusNames=EF_0198;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
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}.
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DR   EMBL; AE016830; AAO80068.1; -; Genomic_DNA.
DR   RefSeq; NP_813997.1; NC_004668.1.
DR   RefSeq; WP_002356190.1; NZ_KE136524.1.
DR   PDB; 6WUB; EM; 3.20 A; l=2-137.
DR   PDB; 7P7R; EM; 2.90 A; m=1-137.
DR   PDBsum; 6WUB; -.
DR   PDBsum; 7P7R; -.
DR   AlphaFoldDB; Q839H1; -.
DR   SMR; Q839H1; -.
DR   STRING; 226185.EF_0198; -.
DR   EnsemblBacteria; AAO80068; AAO80068; EF_0198.
DR   GeneID; 60892694; -.
DR   KEGG; efa:EF0198; -.
DR   PATRIC; fig|226185.45.peg.68; -.
DR   eggNOG; COG0048; Bacteria.
DR   HOGENOM; CLU_104295_1_1_9; -.
DR   OMA; SPALEKC; -.
DR   Proteomes; UP000001415; 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   3D-structure; Methylation; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding.
FT   CHAIN           1..137
FT                   /note="30S ribosomal protein S12"
FT                   /id="PRO_0000146223"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         102
FT                   /note="3-methylthioaspartic acid"
FT                   /evidence="ECO:0000250"
FT   HELIX           4..9
FT                   /evidence="ECO:0007829|PDB:6WUB"
FT   HELIX           22..24
FT                   /evidence="ECO:0007829|PDB:6WUB"
FT   STRAND          30..32
FT                   /evidence="ECO:0007829|PDB:6WUB"
FT   STRAND          43..53
FT                   /evidence="ECO:0007829|PDB:6WUB"
FT   STRAND          63..70
FT                   /evidence="ECO:0007829|PDB:6WUB"
FT   STRAND          75..79
FT                   /evidence="ECO:0007829|PDB:6WUB"
FT   STRAND          92..97
FT                   /evidence="ECO:0007829|PDB:6WUB"
FT   STRAND          101..103
FT                   /evidence="ECO:0007829|PDB:6WUB"
FT   STRAND          106..110
FT                   /evidence="ECO:0007829|PDB:6WUB"
FT   STRAND          114..117
FT                   /evidence="ECO:0007829|PDB:6WUB"
FT   TURN            127..131
FT                   /evidence="ECO:0007829|PDB:6WUB"
SQ   SEQUENCE   137 AA;  15277 MW;  EF6DE7883EF8DB56 CRC64;
     MPTINQLVRK PRKSKVEKSD SPALNKGYNS FKKTQTNVNS PQKRGVCTRV GTMTPKKPNS
     ALRKYARVRL SNLIEVTAYI PGIGHNLQEH SVVLLRGGRV KDLPGVRYHI VRGALDTAGV
     NDRKQSRSKY GTKRPKA
 
 
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