ID   RS11_BACSU              Reviewed;         131 AA.
AC   P04969;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=30S ribosomal protein S11 {ECO:0000255|HAMAP-Rule:MF_01310};
DE            Short=BS11;
GN   Name=rpsK {ECO:0000255|HAMAP-Rule:MF_01310}; OrderedLocusNames=BSU01420;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3093467; DOI=10.1128/jb.168.1.65-71.1986;
RA   Suh J.-W., Boylan S.A., Price C.W.;
RT   "Gene for the alpha subunit of Bacillus subtilis RNA polymerase maps in the
RT   ribosomal protein gene cluster.";
RL   J. Bacteriol. 168:65-71(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2496109; DOI=10.1128/jb.171.5.2553-2562.1989;
RA   Boylan S.A., Suh J.-W., Thomas S.M., Price C.W.;
RT   "Gene encoding the alpha core subunit of Bacillus subtilis RNA polymerase
RT   is cotranscribed with the genes for initiation factor 1 and ribosomal
RT   proteins B, S13, S11, and L17.";
RL   J. Bacteriol. 171:2553-2562(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=8635744; DOI=10.1016/0378-1119(95)00757-1;
RA   Suh J.-W., Boylan S.A., Oh S.H., Price C.W.;
RT   "Genetic and transcriptional organization of the Bacillus subtilis spc-
RT   alpha region.";
RL   Gene 169:17-23(1996).
RN   [4]
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   [5]
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   [6] {ECO:0007744|PDB:6HA1, ECO:0007744|PDB:6HA8}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF 1-131 WITH AND WITHOUT
RP   VIRGINIAMYCIN M, INTERACTION WITH VMLR, 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: Located on the platform of the 30S subunit, it bridges
CC       several disparate RNA helices of the 16S rRNA. Forms part of the Shine-
CC       Dalgarno cleft in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01310}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit (PubMed:30126986). Interacts
CC       with proteins S7 and S18. Binds to IF-3 (By similarity). Interacts with
CC       VmlR (PubMed:30126986). Interacts with BrxC (PubMed:33722570).
CC       {ECO:0000255|HAMAP-Rule:MF_01310, ECO:0000269|PubMed:30126986,
CC       ECO:0000269|PubMed:33722570}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS11 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01310}.
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DR   EMBL; M13957; AAA22707.1; -; Genomic_DNA.
DR   EMBL; M26414; AAA22216.1; -; Genomic_DNA.
DR   EMBL; L47971; AAB06825.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11918.1; -; Genomic_DNA.
DR   PIR; D32307; R3BSS1.
DR   RefSeq; NP_388023.1; NC_000964.3.
DR   RefSeq; WP_009966385.1; NZ_JNCM01000029.1.
DR   PDB; 3J9W; EM; 3.90 A; AK=1-131.
DR   PDB; 5NJT; EM; 3.80 A; K=12-129.
DR   PDB; 6HA1; EM; 3.10 A; k=1-131.
DR   PDB; 6HA8; EM; 3.50 A; k=1-131.
DR   PDB; 6HTQ; EM; 4.50 A; k=18-131.
DR   PDB; 7O5B; EM; 3.33 A; K=1-131.
DR   PDB; 7QV1; EM; 3.50 A; k=1-131.
DR   PDB; 7QV2; EM; 3.50 A; k=1-131.
DR   PDB; 7QV3; EM; 5.14 A; k=1-131.
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; P04969; -.
DR   SMR; P04969; -.
DR   IntAct; P04969; 1.
DR   MINT; P04969; -.
DR   STRING; 224308.BSU01420; -.
DR   jPOST; P04969; -.
DR   PaxDb; P04969; -.
DR   PRIDE; P04969; -.
DR   EnsemblBacteria; CAB11918; CAB11918; BSU_01420.
DR   GeneID; 938926; -.
DR   KEGG; bsu:BSU01420; -.
DR   PATRIC; fig|224308.179.peg.146; -.
DR   eggNOG; COG0100; Bacteria.
DR   InParanoid; P04969; -.
DR   OMA; KWGVAHI; -.
DR   PhylomeDB; P04969; -.
DR   BioCyc; BSUB:BSU01420-MON; -.
DR   PRO; PR:P04969; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0048027; F:mRNA 5'-UTR binding; IBA:GO_Central.
DR   GO; GO:0070181; F:small ribosomal subunit rRNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IBA:GO_Central.
DR   Gene3D; 3.30.420.80; -; 1.
DR   HAMAP; MF_01310; Ribosomal_S11; 1.
DR   InterPro; IPR001971; Ribosomal_S11.
DR   InterPro; IPR019981; Ribosomal_S11_bac-type.
DR   InterPro; IPR018102; Ribosomal_S11_CS.
DR   InterPro; IPR036967; Ribosomal_S11_sf.
DR   PANTHER; PTHR11759; PTHR11759; 1.
DR   Pfam; PF00411; Ribosomal_S11; 1.
DR   PIRSF; PIRSF002131; Ribosomal_S11; 1.
DR   TIGRFAMs; TIGR03632; uS11_bact; 1.
DR   PROSITE; PS00054; RIBOSOMAL_S11; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding.
FT   CHAIN           1..131
FT                   /note="30S ribosomal protein S11"
FT                   /id="PRO_0000123106"
SQ   SEQUENCE   131 AA;  13925 MW;  006838CE7D028781 CRC64;
     MAAARKSNTR KRRVKKNIES GIAHIRSTFN NTIVTITDTH GNAISWSSAG ALGFRGSRKS
     TPFAAQMAAE TAAKGSIEHG LKTLEVTVKG PGSGREAAIR ALQAAGLEVT AIRDVTPVPH
     NGCRPPKRRR V