ID A0A9E8WDF6_9PSED Unreviewed; 206 AA. AC A0A9E8WDF6; DT 03-MAY-2023, integrated into UniProtKB/TrEMBL. DT 03-MAY-2023, sequence version 1. DT 28-JUN-2023, entry version 2. DE RecName: Full=30S ribosomal protein S4 {ECO:0000256|ARBA:ARBA00016779, ECO:0000256|HAMAP-Rule:MF_01306}; GN Name=rpsD {ECO:0000256|HAMAP-Rule:MF_01306, GN ECO:0000313|EMBL:WAH59427.1}; GN ORFNames=LZ023_07730 {ECO:0000313|EMBL:WAH59427.1}; OS Pseudomonas sp. T1-3-2. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=2908006 {ECO:0000313|EMBL:WAH59427.1}; RN [1] {ECO:0000313|EMBL:WAH59427.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=T1-3-2 {ECO:0000313|EMBL:WAH59427.1}; RA Tian L.Y.; RT "Analysis of Genome sequence of plant beneficial strain of Pseudomonas RT silvicola sp. nov."; RL Submitted (JAN-2022) 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:0000256|HAMAP-Rule:MF_01306}. CC -!- FUNCTION: With S5 and S12 plays an important role in translational CC accuracy. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01306}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family. CC {ECO:0000256|ARBA:ARBA00007465, ECO:0000256|HAMAP-Rule:MF_01306, CC ECO:0000256|RuleBase:RU003699}. 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; CP093280; WAH59427.1; -; Genomic_DNA. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR CDD; cd00165; S4; 1. DR Gene3D; 3.10.290.10; RNA-binding S4 domain; 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; 30S 40S RIBOSOMAL PROTEIN; 1. DR PANTHER; PTHR11831:SF4; 37S RIBOSOMAL PROTEIN NAM9, MITOCHONDRIAL; 1. DR Pfam; PF00163; Ribosomal_S4; 1. DR Pfam; PF01479; S4; 1. DR SMART; SM01390; Ribosomal_S4; 1. DR SMART; SM00363; S4; 1. DR SUPFAM; SSF55174; Alpha-L RNA-binding motif; 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 {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP- KW Rule:MF_01306}; KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP- KW Rule:MF_01306}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP- KW Rule:MF_01306}; KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP- KW Rule:MF_01306}. FT DOMAIN 3..95 FT /note="Ribosomal protein S4/S9 N-terminal" FT /evidence="ECO:0000259|SMART:SM01390" FT DOMAIN 96..161 FT /note="RNA-binding S4" FT /evidence="ECO:0000259|SMART:SM00363" SQ SEQUENCE 206 AA; 23059 MW; 7C95EFC3D5B14E1B CRC64; MARYIGPKCK LARREGTDLF LKSGVRALES KCNIEAAPGI HGQRRGRQSD YGTQLREKQK VRRIYGVLER QFSGYYKEAA GKKGATGENL LQLLECRLDN VVYRMGFGAT RAESRQLVSH KAISVNGKTV NVPSYQVRQG DVVAVREKSQ NQLRIVQALE LCAQRGRVEW VDVDTAKKSG VFKNVPARSD LSADINESLI VELYSK //