RS4_TROWT
ID RS4_TROWT Reviewed; 205 AA.
AC Q83GC9;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306};
GN Name=rpsD {ECO:0000255|HAMAP-Rule:MF_01306}; OrderedLocusNames=TWT_378;
OS Tropheryma whipplei (strain Twist) (Whipple's bacillus).
OC Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX NCBI_TaxID=203267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Twist;
RX PubMed=12902375; DOI=10.1101/gr.1474603;
RA Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M.,
RA Claverie J.-M.;
RT "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a
RT reduced genome.";
RL Genome Res. 13:1800-1809(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO44475.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014184; AAO44475.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011096343.1; NC_004572.3.
DR AlphaFoldDB; Q83GC9; -.
DR SMR; Q83GC9; -.
DR STRING; 203267.TWT_378; -.
DR EnsemblBacteria; AAO44475; AAO44475; TWT_378.
DR GeneID; 67388170; -.
DR KEGG; twh:TWT_378; -.
DR eggNOG; COG0522; Bacteria.
DR HOGENOM; CLU_092403_0_3_11; -.
DR OMA; PVICDEQ; -.
DR OrthoDB; 1211060at2; -.
DR Proteomes; UP000002200; 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..205
FT /note="30S ribosomal protein S4"
FT /id="PRO_0000132488"
FT DOMAIN 91..149
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01306"
SQ SEQUENCE 205 AA; 22975 MW; 20FF2F636F25C2E5 CRC64;
MSSCSRTRLS RALGVPLTPK AARLMEVRPY PPGQHGRFRR KGDSDYAVRL REKQRLRGQY
GLREKQLASV YHEARRVKGL AGENLVEMLE MRLDALVLRA AFARSISQAR QLVVHRHILV
DGKLVDRPSY SVSPGQTVKV KPKSVPLDPF QVAASGGHAD VLPPIPGYIE ADLEGLSFRL
VRRPKRSEVP VTCNVQLVVE YYAAR
