RS12_MYCLE
ID RS12_MYCLE Reviewed; 124 AA.
AC P30766;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 3.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=30S ribosomal protein S12 {ECO:0000255|HAMAP-Rule:MF_00403};
GN Name=rpsL {ECO:0000255|HAMAP-Rule:MF_00403}; OrderedLocusNames=ML1880;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8446028; DOI=10.1111/j.1365-2958.1993.tb01112.x;
RA Honore N.T., Bergh S., Chanteau S., Doucet-Populaire F., Eiglmeier K.,
RA Garnier T., Georges C., Launois P., Limpaiboon T., Newton S., Niang K.,
RA del Portillo P., Ramesh G.R., Reddi P., Ridel P.R., Sittisombut N.,
RA Wu-Hunter S., Cole S.T.;
RT "Nucleotide sequence of the first cosmid from the Mycobacterium leprae
RT genome project: structure and function of the Rif-Str regions.";
RL Mol. Microbiol. 7:207-214(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Silbak F., Bercovier H.;
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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-89 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=AAA63909.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA78671.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z14314; CAA78671.1; ALT_INIT; Genomic_DNA.
DR EMBL; X80119; CAA56423.1; -; Genomic_DNA.
DR EMBL; X80124; CAA56425.1; -; Genomic_DNA.
DR EMBL; L40409; AAA63909.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL583923; CAC30834.1; -; Genomic_DNA.
DR PIR; B87144; B87144.
DR PIR; S31148; S31148.
DR RefSeq; NP_302270.1; NC_002677.1.
DR RefSeq; WP_010908591.1; NC_002677.1.
DR AlphaFoldDB; P30766; -.
DR SMR; P30766; -.
DR STRING; 272631.ML1880; -.
DR EnsemblBacteria; CAC30834; CAC30834; CAC30834.
DR KEGG; mle:ML1880; -.
DR PATRIC; fig|272631.5.peg.3554; -.
DR Leproma; ML1880; -.
DR eggNOG; COG0048; Bacteria.
DR HOGENOM; CLU_104295_1_2_11; -.
DR OMA; SPALEKC; -.
DR Proteomes; UP000000806; 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..124
FT /note="30S ribosomal protein S12"
FT /id="PRO_0000146263"
FT REGION 105..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 44..49
FT /note="KPNSAL -> NRTRR (in Ref. 3; AAA63909)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="A -> R (in Ref. 1; CAA78671)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 124 AA; 13862 MW; B53E2434A6F0C123 CRC64;
MPTIQQLVRK GRRDKIGKVK TAALKGNPQR RGVCTRVYTS TPKKPNSALR KVARVKLTSQ
VEVTAYIPGE GHNLQEHSMV LVRGGRVKDL PGVRYKIIRG SLDTQGVKNR KQARSRYGAK
KEKS
