ID RS4_ACIF5 Reviewed; 208 AA.
AC B5EM98;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Small ribosomal subunit protein uS4 {ECO:0000255|HAMAP-Rule:MF_01306};
DE AltName: Full=30S ribosomal protein S4 {ECO:0000305};
GN Name=rpsD {ECO:0000255|HAMAP-Rule:MF_01306}; OrderedLocusNames=Lferr_0523;
OS Acidithiobacillus ferrooxidans (strain ATCC 53993 / BNL-5-31)
OS (Leptospirillum ferrooxidans (ATCC 53993)).
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=380394;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53993 / BNL-5-31;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA Borole A.P.;
RT "Complete sequence of Acidithiobacillus ferrooxidans ATCC 53993.";
RL Submitted (AUG-2008) 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; CP001132; ACH82777.1; -; Genomic_DNA.
DR RefSeq; WP_012536098.1; NC_011206.1.
DR AlphaFoldDB; B5EM98; -.
DR SMR; B5EM98; -.
DR GeneID; 66431409; -.
DR KEGG; afe:Lferr_0523; -.
DR eggNOG; COG0522; Bacteria.
DR HOGENOM; CLU_092403_0_2_6; -.
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; RNA-binding S4 domain; 1.
DR HAMAP; MF_01306_B; Ribosomal_uS4_B; 1.
DR InterPro; IPR022801; Ribosomal_uS4.
DR InterPro; IPR005709; Ribosomal_uS4_bac-type.
DR InterPro; IPR001912; Ribosomal_uS4_N.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR NCBIfam; TIGR01017; rpsD_bact; 1.
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 PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..208
FT /note="Small ribosomal subunit protein uS4"
FT /id="PRO_1000140674"
FT DOMAIN 98..159
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01306"
SQ SEQUENCE 208 AA; 23366 MW; AC28660EA98396B8 CRC64;
MAKYTGPSCR LCRREGGKLF LKGEKCFSDK CPVSIRAYAP GQHGQRRGRV SEYGGQLREK
QKIRRIYGVL EGQFRRYFQR ASQARGVTGE LLLRFLELRL DNVAYRLGFG ASRAEARQVV
RHGHILVNGR RVDIPSYQVR AGDVVSVAEA ARTHIRIAAS VEATAGRGFP EWVSMDTTEL
KATIKAVPVR EDMAPDLNEQ VVVELYSK
//
