ID RS4_CORAM Reviewed; 201 AA. AC Q3S664; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 10-FEB-2021, entry version 53. DE RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306}; GN Name=rpsD {ECO:0000255|HAMAP-Rule:MF_01306}; OS Corynebacterium ammoniagenes (Brevibacterium ammoniagenes). OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=1697; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 6872 / DSM 20305 / IAM 1645 / KCTC 1019 / NCTC 2399; RA Ham S.H., Kim J.H., Lee B.R.; RT "Molecular analysis of RNA polymerase alpha operon from Corynebacterium RT ammoniagenes."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DQ157860; AAZ91711.1; -; Genomic_DNA. DR SMR; Q3S664; -. DR PRIDE; Q3S664; -. 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 Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1..201 FT /note="30S ribosomal protein S4" FT /id="PRO_0000228889" FT DOMAIN 91..154 FT /note="S4 RNA-binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01306" SQ SEQUENCE 201 AA; 23510 MW; FD779660D3DE7FB7 CRC64; MARYTGPATR VSRRLRVDLV GGDMAFERRP YPPGQAGRNR IKESEYLLQL QEKQKAKYTY GVLERQFRRY YVEANRQPGK TGDNLVVLLE TRLDNVVYRA GLARTRRQAR QLVSHGHFTV NGKKTNVPSY RVSQYDIIDI RERSRKMEWF EEAQDRLGEA VVPAWLQVVP ESLRILVHQL PERAQIDVPL QEQLIVELYS K //