RS4_POLSJ
ID RS4_POLSJ Reviewed; 207 AA.
AC Q12G78;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-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=Bpro_0500;
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas; unclassified Polaromonas.
OX NCBI_TaxID=296591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500;
RX PubMed=18723656; DOI=10.1128/aem.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
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; CP000316; ABE42464.1; -; Genomic_DNA.
DR RefSeq; WP_011481467.1; NC_007948.1.
DR AlphaFoldDB; Q12G78; -.
DR SMR; Q12G78; -.
DR STRING; 296591.Bpro_0500; -.
DR EnsemblBacteria; ABE42464; ABE42464; Bpro_0500.
DR KEGG; pol:Bpro_0500; -.
DR eggNOG; COG0522; Bacteria.
DR HOGENOM; CLU_092403_0_2_4; -.
DR OMA; NVVFRMG; -.
DR OrthoDB; 1211060at2; -.
DR Proteomes; UP000001983; 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..207
FT /note="30S ribosomal protein S4"
FT /id="PRO_0000293334"
FT DOMAIN 97..158
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01306"
FT REGION 31..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 207 AA; 23359 MW; 448DF0F9F7824702 CRC64;
MARYLGPKAK LSRREGTDLF LKSARRAISD KAKFDSKPGQ HGRTSGTRTS DFGLQLREKQ
KVKRMYGVLE KQFRRYFEEA DRRKGNTGAN LLFILESRLD NVVYRMGFGS TRAEARQLVS
HKAITVNGNS VNIPSYMVKT GDVIAVRDKS KKQTRVTEAL ELAKQVGLPA WVDVNADKGE
GVFKKVPDRD EFAADVNESL IVELYSR