RS4_HALWD
ID RS4_HALWD Reviewed; 175 AA.
AC Q18G54;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306};
GN Name=rps4 {ECO:0000255|HAMAP-Rule:MF_01306}; OrderedLocusNames=HQ_2943A;
OS Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=362976;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16790 / HBSQ001;
RX PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA Pfeiffer F., Oesterhelt D.;
RT "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT limits of water activity.";
RL BMC Genomics 7:169-169(2006).
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; AM180088; CAJ53047.1; -; Genomic_DNA.
DR RefSeq; WP_011572157.1; NC_008212.1.
DR AlphaFoldDB; Q18G54; -.
DR SMR; Q18G54; -.
DR STRING; 362976.HQ_2943A; -.
DR PRIDE; Q18G54; -.
DR EnsemblBacteria; CAJ53047; CAJ53047; HQ_2943A.
DR GeneID; 4194662; -.
DR KEGG; hwa:HQ_2943A; -.
DR eggNOG; arCOG04239; Archaea.
DR HOGENOM; CLU_089738_1_1_2; -.
DR OMA; ARQFITH; -.
DR Proteomes; UP000001975; 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..175
FT /note="30S ribosomal protein S4"
FT /id="PRO_0000293402"
FT DOMAIN 105..169
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01306"
SQ SEQUENCE 175 AA; 19836 MW; 1CB2A5B71E6A8956 CRC64;
MSTGSNTKRY ETPNHPYQGE RIAQEGDLLG RYGLKNKEEL WRTQSELREY RREARRLIGE
AQGDVSVAEA LGEEFLDRLR RYGILSADDD ISKVLGLDVS DILERRLQTI VYRQGLASTP
KQARQFIVHE HITVNGARVT RPSKMVEETE ANAIAFDENS PLADSLHPAR AEGQE