RS4_GEOSE
ID RS4_GEOSE Reviewed; 200 AA.
AC P81288;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=30S ribosomal protein S4;
DE AltName: Full=BS5;
GN Name=rpsD;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND X-RAY CRYSTALLOGRAPHY (1.7
RP ANGSTROMS) OF 42-200.
RX PubMed=9707415; DOI=10.1093/emboj/17.16.4545;
RA Davies C., Gerstner R.B., Draper D.E., Ramakrishnan V., White S.W.;
RT "The crystal structure of ribosomal protein S4 reveals a two-domain
RT molecule with an extensive RNA-binding surface: one domain shows structural
RT homology to the ETS DNA-binding motif.";
RL EMBO J. 17:4545-4558(1998).
RN [2]
RP PROTEIN SEQUENCE OF 2-200.
RX PubMed=1764513; DOI=10.1016/0300-9084(91)90045-3;
RA Arndt E., Scholzen T., Kromer W., Hatakeyama T., Kimura M.;
RT "Primary structures of ribosomal proteins from the archaebacterium
RT Halobacterium marismortui and the eubacterium Bacillus
RT stearothermophilus.";
RL Biochimie 73:657-668(1991).
RN [3]
RP PROTEIN SEQUENCE OF 2-16.
RC STRAIN=DSM 13240 / CIP 106956 / 10;
RX PubMed=4607606; DOI=10.1016/0014-5793(74)80391-1;
RA Yaguchi M., Matheson A.T., Visentin L.P.;
RT "Procaryotic ribosomal proteins: N-terminal sequence homologies and
RT structural correspondence of 30 S ribosomal proteins from Escherichia coli
RT and Bacillus stearothermophilus.";
RL FEBS Lett. 46:296-300(1974).
RN [4]
RP ISOLATION OF STREPTOMYCIN INDEPENDENT STRAINS.
RC STRAIN=799;
RX PubMed=2254291; DOI=10.1128/jb.172.12.7306-7309.1990;
RA Schnier J., Gewitz H.S., Behrens S.E., Lee A., Ginther C., Leighton T.;
RT "Isolation and characterization of Bacillus stearothermophilus 30S and 50S
RT ribosomal protein mutations.";
RL J. Bacteriol. 172:7306-7309(1990).
RN [5]
RP BINDING TO RRNA.
RX PubMed=11401563; DOI=10.1021/bi010026i;
RA Gerstner R.B., Pak Y., Draper D.E.;
RT "Recognition of 16S rRNA by ribosomal protein S4 from Bacillus
RT stearothermophilus.";
RL Biochemistry 40:7165-7173(2001).
RN [6]
RP STRUCTURE BY NMR OF 42-199.
RX PubMed=10493882; DOI=10.1006/jmbi.1999.3061;
RA Markus M.A., Gerstner R.B., Draper D.E., Torchia D.A.;
RT "Refining the overall structure and subdomain orientation of ribosomal
RT protein S4 delta41 with dipolar couplings measured by NMR in uniaxial
RT liquid crystalline phases.";
RL J. Mol. Biol. 292:375-387(1999).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=11063598; DOI=10.1021/bi0013391;
RA Sayers E.W., Gerstner R.B., Draper D.E., Torchia D.A.;
RT "Structural preordering in the N-terminal region of ribosomal protein S4
RT revealed by heteronuclear NMR spectroscopy.";
RL Biochemistry 39:13602-13613(2000).
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. {ECO:0000250}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S5. The
CC interaction surface between S4 and S5 is involved in control of
CC translational fidelity (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC {ECO:0000305}.
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DR PDB; 1C05; NMR; -; A=43-200.
DR PDB; 1C06; NMR; -; A=43-200.
DR PDBsum; 1C05; -.
DR PDBsum; 1C06; -.
DR AlphaFoldDB; P81288; -.
DR BMRB; P81288; -.
DR SMR; P81288; -.
DR IntAct; P81288; 1.
DR EvolutionaryTrace; P81288; -.
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:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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; Antibiotic resistance; Direct protein sequencing;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1764513,
FT ECO:0000269|PubMed:4607606"
FT CHAIN 2..200
FT /note="30S ribosomal protein S4"
FT /id="PRO_0000132338"
FT DOMAIN 92..152
FT /note="S4 RNA-binding"
FT REGION 22..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 41
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 46..59
FT /evidence="ECO:0007829|PDB:1C05"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1C05"
FT HELIX 65..75
FT /evidence="ECO:0007829|PDB:1C05"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1C05"
FT HELIX 82..92
FT /evidence="ECO:0007829|PDB:1C05"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:1C05"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:1C06"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:1C05"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1C05"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:1C05"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1C05"
FT HELIX 149..156
FT /evidence="ECO:0007829|PDB:1C05"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:1C05"
FT TURN 169..172
FT /evidence="ECO:0007829|PDB:1C05"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:1C05"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:1C05"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:1C05"
SQ SEQUENCE 200 AA; 23196 MW; 8DBED1D1EE76A3F0 CRC64;
MARYTGPMWK ISRRLGISLS GTGKELQKRP YPPGQHGPGQ RRKLSEYGLQ LQEKQKLRHM
YGVNERQFRK TFEEAGKMPG KHGENFMILL ESRLDNLVYR LGLARTRRQA RQLVTHGHII
VDGSRVNIPS YRVKPGQTIA VREKSRNLQV IKEALEANNY IPDYLSFDPE KMEGTYTRLP
ERSELPAEIN EALIVEFYSR
