ID   RS4_METPE               Reviewed;         181 AA.
AC   B8GEG7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306};
GN   Name=rps4 {ECO:0000255|HAMAP-Rule:MF_01306}; OrderedLocusNames=Mpal_2387;
OS   Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanoregulaceae; Methanosphaerula.
OX   NCBI_TaxID=521011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1556 / DSM 19958 / E1-9c;
RX   PubMed=26543115; DOI=10.1128/genomea.01280-15;
RA   Cadillo-Quiroz H., Browne P., Kyrpides N., Woyke T., Goodwin L., Detter C.,
RA   Yavitt J.B., Zinder S.H.;
RT   "Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a
RT   Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.";
RL   Genome Announc. 3:0-0(2015).
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; CP001338; ACL17668.1; -; Genomic_DNA.
DR   RefSeq; WP_012618987.1; NC_011832.1.
DR   AlphaFoldDB; B8GEG7; -.
DR   SMR; B8GEG7; -.
DR   STRING; 521011.Mpal_2387; -.
DR   EnsemblBacteria; ACL17668; ACL17668; Mpal_2387.
DR   GeneID; 7272109; -.
DR   KEGG; mpl:Mpal_2387; -.
DR   eggNOG; arCOG04239; Archaea.
DR   HOGENOM; CLU_089738_1_1_2; -.
DR   OMA; ARQFITH; -.
DR   OrthoDB; 93256at2157; -.
DR   Proteomes; UP000002457; 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_A; Ribosomal_S4_A; 1.
DR   InterPro; IPR022801; Ribosomal_S4/S9.
DR   InterPro; IPR005710; Ribosomal_S4/S9_euk/arc.
DR   InterPro; IPR001912; Ribosomal_S4/S9_N.
DR   InterPro; IPR022802; Ribosomal_S4_arc.
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; PF01479; S4; 1.
DR   SMART; SM01390; Ribosomal_S4; 1.
DR   SMART; SM00363; S4; 1.
DR   TIGRFAMs; TIGR01018; uS4_arch; 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..181
FT                   /note="30S ribosomal protein S4"
FT                   /id="PRO_1000165412"
FT   DOMAIN          108..177
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01306"
FT   REGION          161..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   181 AA;  21001 MW;  6428C55928FA0A4D CRC64;
     MGYPGKNTKG YEAPKRPFEK QRIEDETRIV IEYGLRNKRE VWRAQSVLRR YRKAARELLA
     FMSQSSDEQQ IATKKEHLLG HLNRIGLLGP DADIGDVLSL KIQQPLERRL QTMVYRQGLA
     RSPKQARQMV THGHIAIAGR RVDIPSYRVP RDQETLISYY GTSPLTSEGH PEIERINKKR
     R