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RS4_THET2
ID   RS4_THET2               Reviewed;         209 AA.
AC   P62664;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=30S ribosomal protein S4;
GN   Name=rpsD; Synonyms=rps4; OrderedLocusNames=TT_C1301;
OS   Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=262724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX   PubMed=15064768; DOI=10.1038/nbt956;
RA   Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA   Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA   Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA   Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT   "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL   Nat. Biotechnol. 22:547-553(2004).
CC   -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC       to 16S rRNA where it helps nucleate assembly of the body and platform
CC       of the 30S subunit. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {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   EMBL; AE017221; AAS81643.1; -; Genomic_DNA.
DR   RefSeq; WP_011173699.1; NC_005835.1.
DR   PDB; 4KVB; X-ray; 4.20 A; D=1-209.
DR   PDB; 4V4I; X-ray; 3.71 A; e=1-209.
DR   PDB; 4V4J; X-ray; 3.83 A; e=1-209.
DR   PDB; 4V63; X-ray; 3.21 A; AD/CD=1-209.
DR   PDB; 4V67; X-ray; 3.00 A; AD/CD=1-209.
DR   PDB; 4V7P; X-ray; 3.62 A; AD/DD=2-209.
DR   PDB; 4V83; X-ray; 3.50 A; AD/CD=2-209.
DR   PDB; 4V84; X-ray; 3.40 A; AD/CD=2-209.
DR   PDB; 4V9J; X-ray; 3.86 A; AD/CD=2-209.
DR   PDB; 4V9K; X-ray; 3.50 A; AD/CD=2-209.
DR   PDB; 4V9L; X-ray; 3.50 A; AD/CD=2-209.
DR   PDB; 4V9M; X-ray; 4.00 A; AD/CD=2-209.
DR   PDB; 4V9N; X-ray; 3.40 A; AD/CD=2-209.
DR   PDB; 4V9Q; X-ray; 3.40 A; BD/DD=2-209.
DR   PDB; 4W29; X-ray; 3.80 A; AD/CD=2-209.
DR   PDB; 4XEJ; X-ray; 3.80 A; AS04/BS04=2-209.
DR   PDB; 5J4D; X-ray; 3.10 A; MA/RC=1-209.
DR   PDBsum; 4KVB; -.
DR   PDBsum; 4V4I; -.
DR   PDBsum; 4V4J; -.
DR   PDBsum; 4V63; -.
DR   PDBsum; 4V67; -.
DR   PDBsum; 4V7P; -.
DR   PDBsum; 4V83; -.
DR   PDBsum; 4V84; -.
DR   PDBsum; 4V9J; -.
DR   PDBsum; 4V9K; -.
DR   PDBsum; 4V9L; -.
DR   PDBsum; 4V9M; -.
DR   PDBsum; 4V9N; -.
DR   PDBsum; 4V9Q; -.
DR   PDBsum; 4W29; -.
DR   PDBsum; 4XEJ; -.
DR   PDBsum; 5J4D; -.
DR   AlphaFoldDB; P62664; -.
DR   SMR; P62664; -.
DR   IntAct; P62664; 4.
DR   STRING; 262724.TT_C1301; -.
DR   EnsemblBacteria; AAS81643; AAS81643; TT_C1301.
DR   GeneID; 3168006; -.
DR   KEGG; tth:TT_C1301; -.
DR   eggNOG; COG0522; Bacteria.
DR   HOGENOM; CLU_092403_0_1_0; -.
DR   OMA; NVVFRMG; -.
DR   OrthoDB; 1211060at2; -.
DR   EvolutionaryTrace; P62664; -.
DR   Proteomes; UP000000592; Chromosome.
DR   GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
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; Metal-binding; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..209
FT                   /note="30S ribosomal protein S4"
FT                   /id="PRO_0000132482"
FT   DOMAIN          100..162
FT                   /note="S4 RNA-binding"
FT   ZN_FING         9..31
FT                   /note="C4-type"
FT   BINDING         9
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         12
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         26
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         31
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   TURN            9..11
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   HELIX           12..15
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   HELIX           24..27
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   TURN            33..35
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   TURN            41..43
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   STRAND          44..46
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   HELIX           53..68
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   HELIX           72..84
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   STRAND          85..87
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   HELIX           89..99
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   HELIX           101..107
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   STRAND          109..113
FT                   /evidence="ECO:0007829|PDB:4V63"
FT   HELIX           114..122
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   STRAND          126..132
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   STRAND          145..148
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   HELIX           150..153
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   HELIX           156..163
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   STRAND          165..167
FT                   /evidence="ECO:0007829|PDB:4V84"
FT   STRAND          174..177
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   TURN            178..181
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   STRAND          182..185
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   HELIX           191..193
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   HELIX           200..206
FT                   /evidence="ECO:0007829|PDB:4V67"
SQ   SEQUENCE   209 AA;  24324 MW;  0FF3911816971236 CRC64;
     MGRYIGPVCR LCRREGVKLY LKGERCYSPK CAMERRPYPP GQHGQKRARR PSDYAVRLRE
     KQKLRRIYGI SERQFRNLFE EASKKKGVTG SVFLGLLESR LDNVVYRLGF AVSRRQARQL
     VRHGHITVNG RRVDLPSYRV RPGDEIAVAE KSRNLELIRQ NLEAMKGRKV GPWLSLDVEG
     MKGKFLRLPD REDLALPVNE QLVIEFYSR
 
 
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