RS4_BUCBP
ID RS4_BUCBP Reviewed; 206 AA.
AC P59491;
DT 04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306};
GN Name=rpsD {ECO:0000255|HAMAP-Rule:MF_01306}; OrderedLocusNames=bbp_443;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO27149.1; -; Genomic_DNA.
DR RefSeq; WP_011091550.1; NC_004545.1.
DR AlphaFoldDB; P59491; -.
DR SMR; P59491; -.
DR STRING; 224915.bbp_443; -.
DR EnsemblBacteria; AAO27149; AAO27149; bbp_443.
DR GeneID; 56470978; -.
DR KEGG; bab:bbp_443; -.
DR eggNOG; COG0522; Bacteria.
DR HOGENOM; CLU_092403_0_2_6; -.
DR OMA; NVVFRMG; -.
DR OrthoDB; 1211060at2; -.
DR Proteomes; UP000000601; 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..206
FT /note="30S ribosomal protein S4"
FT /id="PRO_0000132355"
FT DOMAIN 96..156
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01306"
SQ SEQUENCE 206 AA; 23932 MW; 2864E99771AA76DF CRC64;
MAKYLGPKLK LCRRENTDLF FKSGIRAIDS KCKFDQFPGQ HGSKRQRLSD YGVQLREKQK
VRRLYGILEA QFRNYYKHAS RLKGNTGENL LFLLENRLDN VTYRIGFGST RAEARQLVSH
KSILVNNCTV NIPSYQVSPG DVISIHKNSK LQSRIKAALE LSEQRETPIW IEVDFNKMQG
IYKRVPERSD LSAEINEYLI IELYSK