RS12_MYCS2
ID RS12_MYCS2 Reviewed; 124 AA.
AC A0QS96; I7FG33; P41195;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=30S ribosomal protein S12;
GN Name=rpsL; OrderedLocusNames=MSMEG_1398, MSMEI_1360;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-96.
RX PubMed=8192450; DOI=10.1128/aac.38.2.238;
RA Honore N., Cole S.T.;
RT "Streptomycin resistance in mycobacteria.";
RL Antimicrob. Agents Chemother. 38:238-242(1994).
CC -!- FUNCTION: With S4 and S5 plays an important role in translational
CC accuracy. {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S8 and
CC S17. May interact with IF1 in the 30S initiation complex (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS12 family.
CC {ECO:0000305}.
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DR EMBL; CP000480; ABK73485.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37833.1; -; Genomic_DNA.
DR EMBL; X80125; CAB56849.1; -; Genomic_DNA.
DR RefSeq; WP_007167812.1; NZ_SIJM01000030.1.
DR RefSeq; YP_885784.1; NC_008596.1.
DR PDB; 5O5J; EM; 3.45 A; L=1-124.
DR PDB; 5O61; EM; 3.31 A; BL=1-124.
DR PDB; 5XYU; EM; 3.45 A; L=1-124.
DR PDB; 5ZEB; EM; 3.40 A; l=1-124.
DR PDB; 5ZEP; EM; 3.40 A; l=1-124.
DR PDB; 5ZEU; EM; 3.70 A; l=1-124.
DR PDB; 6DZI; EM; 3.46 A; u=2-123.
DR PDB; 6DZK; EM; 3.60 A; L=1-124.
DR PDBsum; 5O5J; -.
DR PDBsum; 5O61; -.
DR PDBsum; 5XYU; -.
DR PDBsum; 5ZEB; -.
DR PDBsum; 5ZEP; -.
DR PDBsum; 5ZEU; -.
DR PDBsum; 6DZI; -.
DR PDBsum; 6DZK; -.
DR AlphaFoldDB; A0QS96; -.
DR SMR; A0QS96; -.
DR IntAct; A0QS96; 2.
DR STRING; 246196.MSMEI_1360; -.
DR PRIDE; A0QS96; -.
DR EnsemblBacteria; ABK73485; ABK73485; MSMEG_1398.
DR EnsemblBacteria; AFP37833; AFP37833; MSMEI_1360.
DR GeneID; 66732857; -.
DR KEGG; msg:MSMEI_1360; -.
DR KEGG; msm:MSMEG_1398; -.
DR PATRIC; fig|246196.19.peg.1381; -.
DR eggNOG; COG0048; Bacteria.
DR OMA; SPALEKC; -.
DR OrthoDB; 1707228at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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..124
FT /note="30S ribosomal protein S12"
FT /id="PRO_0000293603"
FT REGION 105..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 89
FT /note="3-methylthioaspartic acid"
FT /evidence="ECO:0000250"
FT HELIX 4..9
FT /evidence="ECO:0007829|PDB:5XYU"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:5O5J"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:5XYU"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:5XYU"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:5XYU"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:5XYU"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:5O5J"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:5XYU"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:5O5J"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:5XYU"
FT TURN 114..118
FT /evidence="ECO:0007829|PDB:5XYU"
SQ SEQUENCE 124 AA; 13863 MW; 669BE4F3AD829616 CRC64;
MPTIQQLVRK GRRDKIAKVK TAALKGSPQR RGVCTRVYTT TPKKPNSALR KVARVKLTSQ
VEVTAYIPGE GHNLQEHSMV LVRGGRVKDL PGVRYKIIRG SLDTQGVKNR KQARSRYGAK
KEKS
