RS12_MYCPN
ID RS12_MYCPN Reviewed; 139 AA.
AC P75546;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=30S ribosomal protein S12 {ECO:0000255|HAMAP-Rule:MF_00403};
GN Name=rpsL {ECO:0000255|HAMAP-Rule:MF_00403}; OrderedLocusNames=MPN_225;
GN ORFNames=MP606;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
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 -!- CAUTION: Because the enzyme that would modify Asp-102 to 3-
CC methylthioaspartic acid has not been found in the proteome of this
CC organism, that modification is not predicted. {ECO:0000305}.
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DR EMBL; U00089; AAB96254.1; -; Genomic_DNA.
DR PIR; S73932; S73932.
DR RefSeq; NP_109913.1; NC_000912.1.
DR RefSeq; WP_010874582.1; NC_000912.1.
DR AlphaFoldDB; P75546; -.
DR SMR; P75546; -.
DR IntAct; P75546; 6.
DR STRING; 272634.MPN_225; -.
DR EnsemblBacteria; AAB96254; AAB96254; MPN_225.
DR KEGG; mpn:MPN_225; -.
DR PATRIC; fig|272634.6.peg.244; -.
DR HOGENOM; CLU_104295_1_2_14; -.
DR OMA; SPALEKC; -.
DR BioCyc; MPNE272634:G1GJ3-361-MON; -.
DR Proteomes; UP000000808; 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 3: Inferred from homology;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding; tRNA-binding.
FT CHAIN 1..139
FT /note="30S ribosomal protein S12"
FT /id="PRO_0000146268"
SQ SEQUENCE 139 AA; 15629 MW; ADCF0F238AEDF3B4 CRC64;
MATIAQLIRK PRKKKKVKSK SPALHYNLNL LNKKVTNVYS PLKRGVCTRV GTMTPKKPNS
ALRKYAKVRL TNGFEVLTYI PGEGHNLQEH SVTLLRGGRV KDLPGVRYHI VRGTLDTVGV
EKRRQQRSAY GAKKPKAKS
