ID RS12_BRUSU Reviewed; 123 AA.
AC P63194; G0KAF9; Q8YHP5;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=Small ribosomal subunit protein uS12 {ECO:0000255|HAMAP-Rule:MF_00403};
DE AltName: Full=30S ribosomal protein S12 {ECO:0000305};
GN Name=rpsL {ECO:0000255|HAMAP-Rule:MF_00403};
GN OrderedLocusNames=BR1238, BS1330_I1234;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
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}.
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DR EMBL; AE014291; AAN30157.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM18575.1; -; Genomic_DNA.
DR RefSeq; WP_002964366.1; NZ_KN046804.1.
DR AlphaFoldDB; P63194; -.
DR SMR; P63194; -.
DR GeneID; 75497418; -.
DR KEGG; bms:BR1238; -.
DR KEGG; bsi:BS1330_I1234; -.
DR PATRIC; fig|204722.21.peg.3395; -.
DR HOGENOM; CLU_104295_1_2_5; -.
DR PRO; PR:P63194; -.
DR Proteomes; UP000007104; Chromosome I.
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; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_00403_B; Ribosomal_uS12_B; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR006032; Ribosomal_uS12.
DR InterPro; IPR005679; Ribosomal_uS12_bac.
DR NCBIfam; TIGR00981; rpsL_bact; 1.
DR PANTHER; PTHR11652:SF1; 28S RIBOSOMAL PROTEIN S12, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11652; 30S RIBOSOMAL PROTEIN S12 FAMILY MEMBER; 1.
DR Pfam; PF00164; Ribosom_S12_S23; 1.
DR PIRSF; PIRSF002133; Ribosomal_S12/S23; 1.
DR PRINTS; PR01034; RIBOSOMALS12.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 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..123
FT /note="Small ribosomal subunit protein uS12"
FT /id="PRO_0000146191"
FT MOD_RES 89
FT /note="3-methylthioaspartic acid"
FT /evidence="ECO:0000250"
SQ SEQUENCE 123 AA; 13871 MW; 183E267BBD72B54B CRC64;
MPTVNQLIRK PRTAPVKRNK VPALQANPQK RGVCTRVYTT TPKKPNSALR KVAKVRLTNG
FEVIGYIPGE GHNLQEHSVV MIRGGRVKDL PGVRYHIIRG VLDTQGVKNR KQRRSKYGAK
RPK
//
