RS4_LIMRD
ID RS4_LIMRD Reviewed; 201 AA.
AC A5VIU4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306};
GN Name=rpsD {ECO:0000255|HAMAP-Rule:MF_01306}; OrderedLocusNames=Lreu_0500;
OS Limosilactobacillus reuteri (strain DSM 20016) (Lactobacillus reuteri).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=557436;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20016;
RX PubMed=21379339; DOI=10.1371/journal.pgen.1001314;
RA Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M.,
RA Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M.,
RA Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L., Ivanova N.,
RA Kyrpides N.C., Walter J.;
RT "The evolution of host specialization in the vertebrate gut symbiont
RT Lactobacillus reuteri.";
RL PLoS Genet. 7:E1001314-E1001314(2011).
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; CP000705; ABQ82768.1; -; Genomic_DNA.
DR RefSeq; WP_003666632.1; NZ_AZDD01000007.1.
DR AlphaFoldDB; A5VIU4; -.
DR SMR; A5VIU4; -.
DR STRING; 557436.Lreu_0500; -.
DR PRIDE; A5VIU4; -.
DR EnsemblBacteria; ABQ82768; ABQ82768; Lreu_0500.
DR GeneID; 66470620; -.
DR KEGG; lre:Lreu_0500; -.
DR PATRIC; fig|557436.17.peg.1780; -.
DR eggNOG; COG0522; Bacteria.
DR HOGENOM; CLU_092403_0_1_9; -.
DR OMA; NVVFRMG; -.
DR Proteomes; UP000001991; 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; 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 3: Inferred from homology;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..201
FT /note="30S ribosomal protein S4"
FT /id="PRO_0000322309"
FT DOMAIN 93..156
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01306"
FT REGION 26..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 201 AA; 22943 MW; 3055C48C946C8BA9 CRC64;
MSRYTGPSWR VSRRLGVSLS GTGKELARRA YAPGDHGRDR RGKLSEYGTQ LREKQKLRFM
YGMTERQFSN LFVRAGKIKE GTHGANFMAL LERRLDNMVY RLGLATTRRQ ARQLVNHGHI
TVDGKRVDIP SYEVKVGQII AVRDKSKNLD IIKNAVEAVV SRPSYVDFDA DKLEGKLNRI
PAREDMNADI DEALIVEFYN K