RS4_DESHY
ID RS4_DESHY Reviewed; 208 AA.
AC Q250K5;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306};
GN Name=rpsD {ECO:0000255|HAMAP-Rule:MF_01306}; OrderedLocusNames=DSY0498;
OS Desulfitobacterium hafniense (strain Y51).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=138119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y51;
RX PubMed=16513756; DOI=10.1128/jb.188.6.2262-2274.2006;
RA Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT "Complete genome sequence of the dehalorespiring bacterium
RT Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT ethenogenes 195.";
RL J. Bacteriol. 188:2262-2274(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; AP008230; BAE82287.1; -; Genomic_DNA.
DR RefSeq; WP_011459108.1; NC_007907.1.
DR AlphaFoldDB; Q250K5; -.
DR SMR; Q250K5; -.
DR STRING; 138119.DSY0498; -.
DR EnsemblBacteria; BAE82287; BAE82287; DSY0498.
DR KEGG; dsy:DSY0498; -.
DR eggNOG; COG0522; Bacteria.
DR HOGENOM; CLU_092403_0_2_9; -.
DR OMA; NVVFRMG; -.
DR OrthoDB; 1211060at2; -.
DR Proteomes; UP000001946; 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_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; 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; PS50889; S4; 1.
PE 3: Inferred from homology;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..208
FT /note="30S ribosomal protein S4"
FT /id="PRO_0000293270"
FT DOMAIN 99..165
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01306"
SQ SEQUENCE 208 AA; 23895 MW; 00AFA6AEFE0E8EE0 CRC64;
MARYTGPVCR LCRREGMKLF LKGDRCYTGK CAIDRRAYAP GQHGQSRGKK PTEYGIQLRE
KQKVRRIYGV QEKQFRSYYD KANRQKGIVG ENLLRLLERR LDNVVFQLGF ATSRPEARQL
VRHGHFTING RRVDIPSFLV RVGDVVGVKE ASKSSPRLKE ILSSLDRTPP KWMNLDANAA
TGTIIALPDR EDIQLPIQEH LIVEKYSR