RS4_THEVO
ID RS4_THEVO Reviewed; 200 AA.
AC Q97B95;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306};
GN Name=rps4 {ECO:0000255|HAMAP-Rule:MF_01306}; OrderedLocusNames=TV0562;
GN ORFNames=TVG0550709;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(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:0000255|HAMAP-Rule:MF_01306}.
CC -!- FUNCTION: With S5 and S12 plays an important role in translational
CC accuracy. {ECO:0000255|HAMAP-Rule:MF_01306}.
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. {ECO:0000255|HAMAP-Rule:MF_01306}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC {ECO:0000255|HAMAP-Rule:MF_01306}.
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DR EMBL; BA000011; BAB59704.1; -; Genomic_DNA.
DR RefSeq; WP_010916821.1; NC_002689.2.
DR AlphaFoldDB; Q97B95; -.
DR SMR; Q97B95; -.
DR STRING; 273116.14324777; -.
DR EnsemblBacteria; BAB59704; BAB59704; BAB59704.
DR GeneID; 1441079; -.
DR KEGG; tvo:TVG0550709; -.
DR eggNOG; arCOG04239; Archaea.
DR HOGENOM; CLU_089738_1_1_2; -.
DR OMA; ARQFITH; -.
DR OrthoDB; 93256at2157; -.
DR PhylomeDB; Q97B95; -.
DR Proteomes; UP000001017; Chromosome.
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:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00165; S4; 1.
DR Gene3D; 3.10.290.10; -; 1.
DR HAMAP; MF_01306_A; Ribosomal_S4_A; 1.
DR InterPro; IPR022801; Ribosomal_S4/S9.
DR InterPro; IPR005710; Ribosomal_S4/S9_euk/arc.
DR InterPro; IPR001912; Ribosomal_S4/S9_N.
DR InterPro; IPR022802; Ribosomal_S4_arc.
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 Pfam; PF00163; Ribosomal_S4; 1.
DR Pfam; PF01479; S4; 1.
DR SMART; SM01390; Ribosomal_S4; 1.
DR SMART; SM00363; S4; 1.
DR TIGRFAMs; TIGR01018; uS4_arch; 1.
DR PROSITE; PS00632; RIBOSOMAL_S4; 1.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..200
FT /note="30S ribosomal protein S4"
FT /id="PRO_0000132524"
FT DOMAIN 106..170
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01306"
FT REGION 178..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 200 AA; 23161 MW; 71D8DE99D5F122F7 CRC64;
MGDPKFHHKK YSTPRHPWEK DRIDEENKIL VKYGLKNKRE IWRSEAMLSS IRSQARYLRA
RLRASDANAQ KQLERMIKRL SRYKILSDKA TLDDVLSLTV ENILDRRLQT IVFKKNLALS
EKQARQLITH GHITVNGRRV TVPGMLVEAQ YEDTIAYYEN SPIANELHPI RQALLSPAER
VKEEAEKEAA ASEDGGEQDE