RS12_BACSU
ID RS12_BACSU Reviewed; 138 AA.
AC P21472;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 5.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=30S ribosomal protein S12;
DE Short=BS12;
GN Name=rpsL; Synonyms=fun, strA; OrderedLocusNames=BSU01100;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969501; DOI=10.1099/13500872-142-11-3039;
RA Yasumoto K., Liu H., Jeong S.M., Ohashi Y., Kakinuma S., Tanaka K.,
RA Kawamura F., Yoshikawa H., Takahashi H.;
RT "Sequence analysis of a 50 kb region between spo0H and rrnH on the Bacillus
RT subtilis chromosome.";
RL Microbiology 142:3039-3046(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO 102; 105 AND 128, AND LACK OF MODIFICATION.
RC STRAIN=168;
RA Ochi K., Takashi I., Forbes A., Kelleher N.L., Garavelli J.S.;
RL Unpublished observations (AUG-2002).
RN [4]
RP SEQUENCE REVISION TO 102 AND 105.
RC STRAIN=168 / BGSC1A1, and ATCC 21332 / IAM 1213;
RX PubMed=16484214; DOI=10.1128/jb.188.5.2020-2023.2006;
RA Carr J.F., Hamburg D.M., Gregory S.T., Limbach P.A., Dahlberg A.E.;
RT "Effects of streptomycin resistance mutations on posttranslational
RT modification of ribosomal protein S12.";
RL J. Bacteriol. 188:2020-2023(2006).
RN [5]
RP SEQUENCE REVISION TO 102; 105 AND 128, AND LACK OF MODIFICATION.
RC STRAIN=168;
RX PubMed=19653700; DOI=10.1021/pr801114k;
RA Lauber M.A., Running W.E., Reilly J.P.;
RT "B. subtilis ribosomal proteins: structural homology and post-translational
RT modifications.";
RL J. Proteome Res. 8:4193-4206(2009).
RN [6]
RP SEQUENCE REVISION TO 102; 105 AND 128.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=7657605; DOI=10.1074/jbc.270.35.20329;
RA Boor K.J., Duncan M.L., Price C.W.;
RT "Genetic and transcriptional organization of the region encoding the beta
RT subunit of Bacillus subtilis RNA polymerase.";
RL J. Biol. Chem. 270:20329-20336(1995).
RN [8]
RP PROTEIN SEQUENCE OF 2-21.
RX PubMed=6806564; DOI=10.1007/bf00330792;
RA Higo K., Otaka E., Osawa S.;
RT "Purification and characterization of 30S ribosomal proteins from Bacillus
RT subtilis: correlation to Escherichia coli 30S proteins.";
RL Mol. Gen. Genet. 185:239-244(1982).
RN [9]
RP VARIANT STREPTOMYCIN RESISTANT RPSL4 (STRA1) ILE-56, ANTIBIOTIC PRODUCTION,
RP AND MUTAGENESIS OF LYS-56.
RC STRAIN=168;
RX PubMed=9687404; DOI=10.1128/aac.42.8.2041;
RA Hosoya Y., Okamoto S., Muramatsu H., Ochi K.;
RT "Acquisition of certain streptomycin-resistant (str) mutations enhances
RT antibiotic production in bacteria.";
RL Antimicrob. Agents Chemother. 42:2041-2047(1998).
RN [10]
RP CHARACTERIZATION, MUTAGENESIS, AND VARIANTS STREPTOMYCIN RESISTANT RPSL4
RP (STRA1) ILE-56 AND RPSL1 (KO-267) ARG-56.
RC STRAIN=168;
RX PubMed=11489846; DOI=10.1128/jb.183.17.4958-4963.2001;
RA Inaoka T., Kasai K., Ochi K.;
RT "Construction of an in vivo nonsense readthrough assay system and
RT functional analysis of ribosomal proteins S12, S4, and S5 in Bacillus
RT subtilis.";
RL J. Bacteriol. 183:4958-4963(2001).
RN [11]
RP INTERACTION WITH BRXC, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=168 / CU1065 {ECO:0000303|PubMed:33722570};
RX PubMed=33722570; DOI=10.1016/j.redox.2021.101935;
RA Gaballa A., Su T.T., Helmann J.D.;
RT "The Bacillus subtilis monothiol bacilliredoxin BrxC (YtxJ) and the Bdr
RT (YpdA) disulfide reductase reduce S-bacillithiolated proteins.";
RL Redox Biol. 42:101935-101935(2021).
RN [12] {ECO:0007744|PDB:6HA1, ECO:0007744|PDB:6HA8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF 1-138 WITH AND WITHOUT
RP VIRGINIAMYCIN M, AND SUBUNIT.
RX PubMed=30126986; DOI=10.1073/pnas.1808535115;
RA Crowe-McAuliffe C., Graf M., Huter P., Takada H., Abdelshahid M.,
RA Novacek J., Murina V., Atkinson G.C., Hauryliuk V., Wilson D.N.;
RT "Structural basis for antibiotic resistance mediated by the Bacillus
RT subtilis ABCF ATPase VmlR.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:8978-8983(2018).
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 (By similarity). {ECO:0000255|HAMAP-
CC Rule:MF_00403}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit (PubMed:30126986). Contacts
CC proteins S8 and S17. May interact with IF1 in the 30S initiation
CC complex (By similarity). Interacts with BrxC (PubMed:33722570).
CC {ECO:0000255|HAMAP-Rule:MF_00403, ECO:0000269|PubMed:30126986,
CC ECO:0000269|PubMed:33722570}.
CC -!- MISCELLANEOUS: Many streptomycin resistant B.subtilis with mutations in
CC this protein produce increased quantities of a natural (but
CC uncharacterized) antibiotic. {ECO:0000269|PubMed:9687404}.
CC -!- MISCELLANEOUS: A number of substitutions and deletions can promote
CC streptomycin resistance, dependence or pseudodependence; all but one of
CC these (K55R) are associated with hyperaccurate translation.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS12 family.
CC {ECO:0000305}.
CC -!- CAUTION: The enzyme that would modify Asp-102 to 3-methylthioaspartic
CC acid has not been found in the proteome of this organism, and that
CC modification does not occur. {ECO:0000305}.
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DR EMBL; D64127; BAA11001.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11886.2; -; Genomic_DNA.
DR EMBL; L43593; AAB59114.1; -; Genomic_DNA.
DR PIR; C69700; C69700.
DR RefSeq; NP_387991.2; NC_000964.3.
DR RefSeq; WP_003225781.1; NZ_JNCM01000029.1.
DR PDB; 3J9W; EM; 3.90 A; AL=1-138.
DR PDB; 5NJT; EM; 3.80 A; L=2-138.
DR PDB; 6HA1; EM; 3.10 A; l=1-138.
DR PDB; 6HA8; EM; 3.50 A; l=1-138.
DR PDB; 6HTQ; EM; 4.50 A; l=2-137.
DR PDB; 7O5B; EM; 3.33 A; L=1-138.
DR PDB; 7QV1; EM; 3.50 A; l=1-138.
DR PDB; 7QV2; EM; 3.50 A; l=1-138.
DR PDB; 7QV3; EM; 5.14 A; l=1-138.
DR PDBsum; 3J9W; -.
DR PDBsum; 5NJT; -.
DR PDBsum; 6HA1; -.
DR PDBsum; 6HA8; -.
DR PDBsum; 6HTQ; -.
DR PDBsum; 7O5B; -.
DR PDBsum; 7QV1; -.
DR PDBsum; 7QV2; -.
DR PDBsum; 7QV3; -.
DR AlphaFoldDB; P21472; -.
DR SMR; P21472; -.
DR STRING; 224308.BSU01100; -.
DR PaxDb; P21472; -.
DR PRIDE; P21472; -.
DR EnsemblBacteria; CAB11886; CAB11886; BSU_01100.
DR GeneID; 64301948; -.
DR GeneID; 936616; -.
DR KEGG; bsu:BSU01100; -.
DR PATRIC; fig|224308.179.peg.113; -.
DR eggNOG; COG0048; Bacteria.
DR InParanoid; P21472; -.
DR OMA; SPALEKC; -.
DR PhylomeDB; P21472; -.
DR BioCyc; BSUB:BSU01100-MON; -.
DR PRO; PR:P21472; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005840; C:ribosome; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
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 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; Antibiotic resistance; Direct protein sequencing;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding; tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6806564"
FT CHAIN 2..138
FT /note="30S ribosomal protein S12"
FT /id="PRO_0000146178"
FT REGION 33..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 102
FT /note="Not modified"
FT /evidence="ECO:0000269|PubMed:19653700, ECO:0000269|Ref.3"
FT VARIANT 56
FT /note="K -> I (in RPSL4 (STRA1); confers streptomycin
FT resistance and hyperaccurate translation, has no effect on
FT natural antibiotic production)"
FT /evidence="ECO:0000269|PubMed:9687404"
FT VARIANT 56
FT /note="K -> R (in RPSL1 (KO-267); confers streptomycin
FT resistance but not hyperaccurate translation, increases
FT natural antibiotic production 10-fold)"
FT /evidence="ECO:0000269|PubMed:11489846,
FT ECO:0000269|PubMed:9687404"
FT MUTAGEN 56
FT /note="K->D: Confers streptomycin resistance and very poor
FT growth in rich medium."
FT /evidence="ECO:0000269|PubMed:11489846"
FT CONFLICT 102
FT /note="D -> N (in Ref. 1; BAA11001)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="G -> R (in Ref. 1; BAA11001)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="S -> P (in Ref. 1; BAA11001)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 138 AA; 15216 MW; 1E8EDCEC75B75648 CRC64;
MPTINQLIRK GRVSKVENSK SPALNKGYNS FKKEHTNVSS PQKRGVCTRV GTMTPKKPNS
ALRKYARVRL TNGIEVTAYI PGIGHNLQEH SVVLIRGGRV KDLPGVRYHI VRGALDTAGV
ENRAQGRSKY GTKKPKAK
