RS4_SYNE7
ID RS4_SYNE7 Reviewed; 202 AA.
AC Q31N52;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306};
GN Name=rpsD {ECO:0000255|HAMAP-Rule:MF_01306};
GN Synonyms=rps4 {ECO:0000255|HAMAP-Rule:MF_01306};
GN OrderedLocusNames=Synpcc7942_1487;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
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}.
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DR EMBL; CP000100; ABB57517.1; -; Genomic_DNA.
DR RefSeq; WP_011244783.1; NC_007604.1.
DR AlphaFoldDB; Q31N52; -.
DR SMR; Q31N52; -.
DR STRING; 1140.Synpcc7942_1487; -.
DR PRIDE; Q31N52; -.
DR EnsemblBacteria; ABB57517; ABB57517; Synpcc7942_1487.
DR KEGG; syf:Synpcc7942_1487; -.
DR eggNOG; COG0522; Bacteria.
DR HOGENOM; CLU_092403_0_5_3; -.
DR OMA; NVVFRMG; -.
DR OrthoDB; 1211060at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1487-MON; -.
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 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..202
FT /note="30S ribosomal protein S4"
FT /id="PRO_0000293389"
FT DOMAIN 90..154
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01306"
FT REGION 23..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 202 AA; 23206 MW; FD587394B089DBC5 CRC64;
MSRYRGPRLR IVRRLGDLPG LTRKAARRSY PPGQHGQARR KRSEYAIRLE EKQKLRFNYG
LSERQLVRYV KKARRMQGST GTNLLQLLEM RLDNLVFRLG FAPTIPGARQ LVNHGHVTVN
GRVVDIASYN CRPGEVIGVR QREASRKLVT ANLEYPGLAN VPVHLDFDKN KLEAKVTGAC
EREWVALQIN ELLVVEYYSR KV
