RS12_MYCAV
ID RS12_MYCAV Reviewed; 124 AA.
AC P51999; Q9R5U7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 25-MAY-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};
OS Mycobacterium avium.
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=1764;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=35713;
RX PubMed=8821605; DOI=10.1093/jac/36.6.1049;
RA Portillo-Gomez L., Nair J., Rouse D.A., Morris S.L.;
RT "The absence of genetic markers for streptomycin and rifampicin resistance
RT in Mycobacterium avium complex strains.";
RL J. Antimicrob. Chemother. 36:1049-1053(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-96.
RC STRAIN=ATCC 2591;
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: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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X80120; CAB56845.1; -; Genomic_DNA.
DR RefSeq; WP_003879423.1; NZ_NSFM01000032.1.
DR AlphaFoldDB; P51999; -.
DR SMR; P51999; -.
DR GeneID; 64259750; -.
DR GeneID; 66695579; -.
DR OMA; SPALEKC; -.
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 Methylation; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding; tRNA-binding.
FT CHAIN 1..124
FT /note="30S ribosomal protein S12"
FT /id="PRO_0000146256"
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 CONFLICT 11
FT /note="G -> V (in Ref. 2; CAB56845)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="I -> V (in Ref. 2; CAB56845)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 124 AA; 13849 MW; 2B29ADD44DFB7188 CRC64;
MPTIQQLVRK GRRDKIGKVK TAALKGSPQR RGVCTRVYTT TPKKPNSALR KVARVKLTSQ
VEVTAYIPGE GHNLQEHSMV LVRGGRVKDL PGVRYKIIRG SLDTQGVKNR KQARSRYGAK
KEKS
