RS4B_SYMTH
ID RS4B_SYMTH Reviewed; 201 AA.
AC Q67T95;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=30S ribosomal protein S4 B {ECO:0000255|HAMAP-Rule:MF_01306};
GN Name=rpsD2 {ECO:0000255|HAMAP-Rule:MF_01306}; Synonyms=rpsD;
GN OrderedLocusNames=STH113;
OS Symbiobacterium thermophilum (strain T / IAM 14863).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC Symbiobacterium.
OX NCBI_TaxID=292459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T / IAM 14863;
RX PubMed=15383646; DOI=10.1093/nar/gkh830;
RA Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA Ikeda H., Hattori M., Beppu T.;
RT "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT that depends on microbial commensalism.";
RL Nucleic Acids Res. 32:4937-4944(2004).
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; AP006840; BAD39098.1; -; Genomic_DNA.
DR RefSeq; WP_011194248.1; NC_006177.1.
DR AlphaFoldDB; Q67T95; -.
DR SMR; Q67T95; -.
DR STRING; 292459.STH113; -.
DR EnsemblBacteria; BAD39098; BAD39098; STH113.
DR KEGG; sth:STH113; -.
DR eggNOG; COG0522; Bacteria.
DR HOGENOM; CLU_092403_0_1_9; -.
DR OMA; HIPFEFN; -.
DR OrthoDB; 1211060at2; -.
DR Proteomes; UP000000417; 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..201
FT /note="30S ribosomal protein S4 B"
FT /id="PRO_0000228932"
FT DOMAIN 93..156
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01306"
SQ SEQUENCE 201 AA; 22874 MW; EBE35A1D0466AE80 CRC64;
MARYIGPKHK LCRRVGRPLC GSAKCPALKR PYRPGQHGPG RPQKLSEYGA QLLEKQKLRF
IYGVMERQFR RYFEQAQRSR GVTGEVLLQL LEQRLDTVVY RLGFARTMAA ARQLVGHGHV
TLNGRRVDIA SCQVKPGDVV GLTQKARSLA VVRESLDLRR PVPPYLSLDE TTMTSRLQRL
PLREEIPVDV DESLVVELYA R