RS12_MYCBO
ID RS12_MYCBO Reviewed; 124 AA.
AC Q53538; A0A1R3XW32; Q9R547; X2BFV8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=30S ribosomal protein S12;
GN Name=rpsL; OrderedLocusNames=BQ2027_MB0701;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BCG;
RX PubMed=7663416;
RA Iwanaga S., Ohara N., Kariu T., Kimura M., Yamasaki N., Yamada T.;
RT "Cloning and nucleotide sequence of the gene cluster encoding ribosomal
RT proteins S12 and S7 from Mycobacterium bovis BCG.";
RL Biochem. Mol. Biol. Int. 36:209-218(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
RN [4]
RP PROTEIN SEQUENCE OF 2-16.
RC STRAIN=BCG;
RX PubMed=8405418; DOI=10.1016/0014-5793(93)80287-5;
RA Ohara N., Kimura M., Higashi Y., Yamada T.;
RT "Isolation and amino acid sequence of the 30S ribosomal protein S19 from
RT Mycobacterium bovis BCG.";
RL FEBS Lett. 331:9-14(1993).
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}.
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}.
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DR EMBL; S79283; AAB35201.2; -; Genomic_DNA.
DR EMBL; LT708304; SIT99299.1; -; Genomic_DNA.
DR PIR; S36888; S36888.
DR RefSeq; NP_854359.1; NC_002945.3.
DR RefSeq; WP_003403453.1; NC_002945.4.
DR AlphaFoldDB; Q53538; -.
DR SMR; Q53538; -.
DR EnsemblBacteria; SIT99299; SIT99299; BQ2027_MB0701.
DR GeneID; 45424644; -.
DR PATRIC; fig|233413.5.peg.764; -.
DR OMA; SPALEKC; -.
DR Proteomes; UP000001419; 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 Direct protein sequencing; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8405418"
FT CHAIN 2..124
FT /note="30S ribosomal protein S12"
FT /id="PRO_0000146257"
FT REGION 105..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 24
FT /note="L -> P (in Ref. 1; AAB35201)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="G -> R (in Ref. 1; AAB35201)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="T -> N (in Ref. 1; AAB35201)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="R -> Q (in Ref. 1; AAB35201)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 124 AA; 13849 MW; 2B441B040CEF20CD CRC64;
MPTIQQLVRK GRRDKISKVK TAALKGSPQR RGVCTRVYTT TPKKPNSALR KVARVKLTSQ
VEVTAYIPGE GHNLQEHSMV LVRGGRVKDL PGVRYKIIRG SLDTQGVKNR KQARSRYGAK
KEKG
