RS4_PICTO
ID RS4_PICTO Reviewed; 183 AA.
AC Q6KZP7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306};
GN Name=rps4 {ECO:0000255|HAMAP-Rule:MF_01306}; OrderedLocusNames=PTO1220;
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=263820;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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; AE017261; AAT43805.1; -; Genomic_DNA.
DR RefSeq; WP_011178021.1; NC_005877.1.
DR AlphaFoldDB; Q6KZP7; -.
DR SMR; Q6KZP7; -.
DR STRING; 263820.PTO1220; -.
DR EnsemblBacteria; AAT43805; AAT43805; PTO1220.
DR GeneID; 2844167; -.
DR KEGG; pto:PTO1220; -.
DR PATRIC; fig|263820.9.peg.1268; -.
DR eggNOG; arCOG04239; Archaea.
DR HOGENOM; CLU_089738_1_1_2; -.
DR OMA; ARQFITH; -.
DR OrthoDB; 93256at2157; -.
DR Proteomes; UP000000438; 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; 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 Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..183
FT /note="30S ribosomal protein S4"
FT /id="PRO_0000132514"
FT DOMAIN 106..168
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01306"
FT REGION 158..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 183 AA; 21620 MW; 63C46F6F5A78C650 CRC64;
MGDQKFQRKK YSTPRHPWEK DRIDAERQLL IKYGLKNKRE LWRAQTILTN FRTQARTLQA
KLRYNDPLAI KQFQLLIGKL SRLNLLGENA TLDDVLSLNI EDILERRLET LVYKKNLALT
MKQARQFITH GHIKVNDRVV TIPSFMVEKS MEDSITYNET SPFTDENHPL RMEMSGTKEE
ENE