RS12_MYCMS
ID RS12_MYCMS Reviewed; 139 AA.
AC Q8VMU2;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=30S ribosomal protein S12 {ECO:0000255|HAMAP-Rule:MF_00403};
GN Name=rpsL {ECO:0000255|HAMAP-Rule:MF_00403};
GN Synonyms=rps12 {ECO:0000255|HAMAP-Rule:MF_00403};
GN OrderedLocusNames=MSC_0157;
OS Mycoplasma mycoides subsp. mycoides SC (strain PG1).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272632;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12383637; DOI=10.1016/s0378-1135(02)00258-4;
RA Martin-Alonso J.M., Prieto M., Parra F.;
RT "Genetic and antigenic characterisation of elongation factor Tu from
RT Mycoplasma mycoides subsp. mycoides SC.";
RL Vet. Microbiol. 89:277-289(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG1;
RX PubMed=14762060; DOI=10.1101/gr.1673304;
RA Westberg J., Persson A., Holmberg A., Goesmann A., Lundeberg J.,
RA Johansson K.-E., Pettersson B., Uhlen M.;
RT "The genome sequence of Mycoplasma mycoides subsp. mycoides SC type strain
RT PG1T, the causative agent of contagious bovine pleuropneumonia (CBPP).";
RL Genome Res. 14:221-227(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 -!- 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE76802.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ345083; CAC87985.1; -; Genomic_DNA.
DR EMBL; AJ419601; CAD21851.1; -; Genomic_DNA.
DR EMBL; BX293980; CAE76802.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_975160.3; NC_005364.2.
DR AlphaFoldDB; Q8VMU2; -.
DR SMR; Q8VMU2; -.
DR STRING; 272632.MSC_0157; -.
DR EnsemblBacteria; CAE76802; CAE76802; MSC_0157.
DR KEGG; mmy:MSC_0157; -.
DR PATRIC; fig|272632.4.peg.166; -.
DR eggNOG; COG0048; Bacteria.
DR HOGENOM; CLU_104295_1_1_14; -.
DR OMA; SPALEKC; -.
DR Proteomes; UP000001016; 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_0000146265"
FT CONFLICT 69
FT /note="R -> I (in Ref. 1; CAC87985/CAD21851)"
FT /evidence="ECO:0000305"
FT CONFLICT 74..76
FT /note="MEV -> VEG (in Ref. 1; CAC87985/CAD21851)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="Q -> R (in Ref. 1; CAC87985/CAD21851)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="S -> R (in Ref. 1; CAC87985/CAD21851)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="T -> A (in Ref. 1; CAC87985/CAD21851)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 139 AA; 15489 MW; 39A9A894A09783A9 CRC64;
MPTINQLVKV NRKAKTWKTK APALNRGINT LIKKVTKIAS PQKRGVCTRV ATMTPKKPNS
ALRKYARVRL TNGMEVNAYI PGEGHNLQEH SVVLIRGGRV KDLPGVRYHV IRGTLDTQGV
AKRSQGRSLY GVKRPKVKK
