ID   RS6_ECO24               Reviewed;         131 AA.
AC   A7ZV71;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=30S ribosomal protein S6 {ECO:0000255|HAMAP-Rule:MF_00360};
GN   Name=rpsF {ECO:0000255|HAMAP-Rule:MF_00360};
GN   OrderedLocusNames=EcE24377A_4761;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
CC   -!- FUNCTION: Binds together with S18 to 16S ribosomal RNA.
CC       {ECO:0000255|HAMAP-Rule:MF_00360}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS6 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00360}.
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DR   EMBL; CP000800; ABV19548.1; -; Genomic_DNA.
DR   RefSeq; WP_001216676.1; NC_009801.1.
DR   AlphaFoldDB; A7ZV71; -.
DR   SMR; A7ZV71; -.
DR   EnsemblBacteria; ABV19548; ABV19548; EcE24377A_4761.
DR   GeneID; 67414819; -.
DR   KEGG; ecw:EcE24377A_4761; -.
DR   HOGENOM; CLU_113441_6_1_6; -.
DR   OMA; ITEASPM; -.
DR   Proteomes; UP000001122; Chromosome.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
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; cd00473; bS6; 1.
DR   Gene3D; 3.30.70.60; -; 1.
DR   HAMAP; MF_00360; Ribosomal_S6; 1.
DR   InterPro; IPR000529; Ribosomal_S6.
DR   InterPro; IPR020815; Ribosomal_S6_CS.
DR   InterPro; IPR020814; Ribosomal_S6_plastid/chlpt.
DR   InterPro; IPR035980; Ribosomal_S6_sf.
DR   InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6.
DR   PANTHER; PTHR21011; PTHR21011; 1.
DR   Pfam; PF01250; Ribosomal_S6; 1.
DR   SUPFAM; SSF54995; SSF54995; 1.
DR   TIGRFAMs; TIGR00166; S6; 1.
DR   PROSITE; PS01048; RIBOSOMAL_S6; 1.
PE   3: Inferred from homology;
KW   Acetylation; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..131
FT                   /note="30S ribosomal protein S6"
FT                   /id="PRO_1000059855"
FT   REGION          98..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..120
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         93
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00360"
SQ   SEQUENCE   131 AA;  15187 MW;  01C1FD0EF4197ED2 CRC64;
     MRHYEIVFMV HPDQSEQVPG MIERYTAAIT GAEGKIHRLE DWGRRQLAYP INKLHKAHYV
     LMNVEAPQEV IDELETTFRF NDAVIRSMVM RTKHAVTEAS PMVKAKDERR ERRDDFANET
     ADDAEAGDSE E