RS4_ECO57
ID RS4_ECO57 Reviewed; 206 AA.
AC P0A7W0; P02354;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=30S ribosomal protein S4;
GN Name=rpsD; Synonyms=ramA; OrderedLocusNames=Z4666, ECs4161;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: One of two assembly initiator proteins for the 30S subunit,
CC it binds directly to 16S rRNA where it nucleates assembly of the body
CC of the 30S subunit. {ECO:0000250}.
CC -!- FUNCTION: With S5 and S12 plays an important role in translational
CC accuracy; many suppressors of streptomycin-dependent mutants of protein
CC S12 are found in this protein, some but not all of which decrease
CC translational accuracy (ram, ribosomal ambiguity mutations).
CC {ECO:0000250}.
CC -!- FUNCTION: Protein S4 is also a translational repressor protein, it
CC controls the translation of the alpha-operon (which codes for S13, S11,
CC S4, RNA polymerase alpha subunit, and L17) by binding to its mRNA.
CC {ECO:0000250}.
CC -!- FUNCTION: Also functions as a rho-dependent antiterminator of rRNA
CC transcription, increasing the synthesis of rRNA under conditions of
CC excess protein, allowing a more rapid return to homeostasis. Binds
CC directly to RNA polymerase (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S5. Some
CC nascent polypeptide chains are able to cross-link to this protein in
CC situ (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC {ECO:0000305}.
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DR EMBL; AE005174; AAG58417.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37584.1; -; Genomic_DNA.
DR PIR; A91149; A91149.
DR PIR; E85994; E85994.
DR RefSeq; NP_312188.1; NC_002695.1.
DR RefSeq; WP_000135224.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0A7W0; -.
DR SMR; P0A7W0; -.
DR STRING; 155864.EDL933_4513; -.
DR EnsemblBacteria; AAG58417; AAG58417; Z4666.
DR EnsemblBacteria; BAB37584; BAB37584; ECs_4161.
DR GeneID; 67415337; -.
DR GeneID; 915983; -.
DR KEGG; ece:Z4666; -.
DR KEGG; ecs:ECs_4161; -.
DR PATRIC; fig|386585.9.peg.4344; -.
DR eggNOG; COG0522; Bacteria.
DR HOGENOM; CLU_092403_0_2_6; -.
DR OMA; NVVFRMG; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
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; Repressor; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; Transcription; Transcription regulation;
KW Transcription termination; Translation regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..206
FT /note="30S ribosomal protein S4"
FT /id="PRO_0000132382"
FT DOMAIN 96..156
FT /note="S4 RNA-binding"
SQ SEQUENCE 206 AA; 23469 MW; 4015969DF8E582BB CRC64;
MARYLGPKLK LSRREGTDLF LKSGVRAIDT KCKIEQAPGQ HGARKPRLSD YGVQLREKQK
VRRIYGVLER QFRNYYKEAA RLKGNTGENL LALLEGRLDN VVYRMGFGAT RAEARQLVSH
KAIMVNGRVV NIASYQVSPN DVVSIREKAK KQSRVKAALE LAEQREKPTW LEVDAGKMEG
TFKRKPERSD LSADINEHLI VELYSK
