RS4_BACSU
ID RS4_BACSU Reviewed; 200 AA.
AC P21466; Q45662; Q53282;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=30S ribosomal protein S4;
DE Short=BS4;
GN Name=rpsD; OrderedLocusNames=BSU29660;
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=1699930; DOI=10.1128/jb.172.11.6372-6379.1990;
RA Grundy F.J., Henkin T.M.;
RT "Cloning and analysis of the Bacillus subtilis rpsD gene, encoding
RT ribosomal protein S4.";
RL J. Bacteriol. 172:6372-6379(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57.
RX PubMed=1906866; DOI=10.1128/jb.173.15.4595-4602.1991;
RA Grundy F.J., Henkin T.M.;
RT "The rpsD gene, encoding ribosomal protein S4, is autogenously regulated in
RT Bacillus subtilis.";
RL J. Bacteriol. 173:4595-4602(1991).
RN [5]
RP PROTEIN SEQUENCE OF 2-25.
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 [6]
RP VARIANTS RPSD2 75-ALA--LEU-78 DEL AND RPSD1 LEU-ALA-GLY-LYS-LEU INS.
RX PubMed=2121712; DOI=10.1128/jb.172.11.6380-6385.1990;
RA Henkin T.M., Chambliss G.H., Grundy F.;
RT "Bacillus subtilis mutants with alterations in ribosomal protein S4.";
RL J. Bacteriol. 172:6380-6385(1990).
RN [7]
RP CHARACTERIZATION, AND VARIANTS RPSD3 LYS-46; RPSD2 75-ALA--LEU-78 DEL AND
RP RPSD1 LEU-ALA-GLY-LYS-LEU INS.
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 [8] {ECO:0007744|PDB:6HA1, ECO:0007744|PDB:6HA8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF 1-200 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: One of the primary rRNA binding proteins, it binds directly
CC to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
CC {ECO:0000250}.
CC -!- FUNCTION: With S5 and S12 plays an important role in translational
CC accuracy; many suppressors of streptomycin-dependent mutants of protein
CC S12 are found in this protein, some but not all of which decrease
CC translational accuracy (ram, ribosomal ambiguity mutations).
CC -!- FUNCTION: S4 represses its own expression; it is not know if this is at
CC the level of translation or of mRNA stability.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit (PubMed:30126986). Contacts
CC protein S5. The interaction surface between S4 and S5 is involved in
CC control of translational fidelity. {ECO:0000269|PubMed:30126986}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC {ECO:0000305}.
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DR EMBL; M59358; AAA22717.1; -; Genomic_DNA.
DR EMBL; AF008220; AAC00397.1; -; Genomic_DNA.
DR EMBL; S45404; AAB19387.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14944.1; -; Genomic_DNA.
DR EMBL; M60889; AAA22716.1; -; Genomic_DNA.
DR PIR; A37146; A37146.
DR RefSeq; NP_390844.1; NC_000964.3.
DR RefSeq; WP_003229304.1; NZ_JNCM01000036.1.
DR PDB; 3J9W; EM; 3.90 A; AD=1-200.
DR PDB; 5NJT; EM; 3.80 A; D=2-200.
DR PDB; 6HA1; EM; 3.10 A; d=1-200.
DR PDB; 6HA8; EM; 3.50 A; d=1-200.
DR PDB; 6HTQ; EM; 4.50 A; d=6-200.
DR PDB; 7O5B; EM; 3.33 A; D=1-200.
DR PDB; 7QV1; EM; 3.50 A; d=1-200.
DR PDB; 7QV2; EM; 3.50 A; d=1-200.
DR PDB; 7QV3; EM; 5.14 A; d=1-200.
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; P21466; -.
DR SMR; P21466; -.
DR IntAct; P21466; 1.
DR MINT; P21466; -.
DR STRING; 224308.BSU29660; -.
DR jPOST; P21466; -.
DR PaxDb; P21466; -.
DR PRIDE; P21466; -.
DR EnsemblBacteria; CAB14944; CAB14944; BSU_29660.
DR GeneID; 937319; -.
DR KEGG; bsu:BSU29660; -.
DR PATRIC; fig|224308.179.peg.3223; -.
DR eggNOG; COG0522; Bacteria.
DR InParanoid; P21466; -.
DR OMA; NVVFRMG; -.
DR PhylomeDB; P21466; -.
DR BioCyc; BSUB:BSU29660-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0045903; P:positive regulation of translational fidelity; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00165; S4; 1.
DR Gene3D; 3.10.290.10; -; 1.
DR HAMAP; MF_01306_B; Ribosomal_S4_B; 1.
DR InterPro; IPR022801; Ribosomal_S4/S9.
DR InterPro; IPR001912; Ribosomal_S4/S9_N.
DR InterPro; IPR005709; Ribosomal_S4_bac-type.
DR InterPro; IPR018079; Ribosomal_S4_CS.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR PANTHER; PTHR11831; PTHR11831; 1.
DR PANTHER; PTHR11831:SF4; PTHR11831:SF4; 1.
DR Pfam; PF00163; Ribosomal_S4; 1.
DR Pfam; PF01479; S4; 1.
DR SMART; SM01390; Ribosomal_S4; 1.
DR SMART; SM00363; S4; 1.
DR TIGRFAMs; TIGR01017; rpsD_bact; 1.
DR PROSITE; PS00632; RIBOSOMAL_S4; 1.
DR PROSITE; PS50889; S4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Reference proteome; Repressor;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6806564"
FT CHAIN 2..200
FT /note="30S ribosomal protein S4"
FT /id="PRO_0000132339"
FT DOMAIN 92..155
FT /note="S4 RNA-binding"
FT REGION 22..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 46
FT /note="E -> K (in rpsD3; suppresses S12 mutation K55D)"
FT /evidence="ECO:0000269|PubMed:11489846"
FT VARIANT 75..78
FT /note="Missing (in rpsD2; suppresses S12 mutation K55D. A
FT ram mutation)"
FT /evidence="ECO:0000269|PubMed:11489846,
FT ECO:0000269|PubMed:2121712"
FT VARIANT 78
FT /note="L -> LAGKL (in rpsD1; suppresses S12 mutation K55D.
FT A ram mutation)"
FT /evidence="ECO:0000269|PubMed:11489846"
SQ SEQUENCE 200 AA; 22835 MW; C4FE9F65A5EB7E34 CRC64;
MARYTGPSWK LSRRLGISLS GTGKELEKRP YAPGPHGPGQ RKKLSEYGLQ LQEKQKLRHM
YGVNERQFRT LFDKAGKLAG KHGENFMILL DSRLDNVVYK LGLARTRRQA RQLVNHGHIL
VDGSRVDIPS YLVKPGQTIG VREKSRNLSI IKESVEVNNF VPEYLTFDAE KLEGTFTRLP
ERSELAPEIN EALIVEFYSR
