ID   RS6_ECOBW               Reviewed;         131 AA.
AC   C4ZR77;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=30S ribosomal protein S6 {ECO:0000255|HAMAP-Rule:MF_00360};
GN   Name=rpsF {ECO:0000255|HAMAP-Rule:MF_00360}; OrderedLocusNames=BWG_3912;
OS   Escherichia coli (strain K12 / MC4100 / BW2952).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=595496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MC4100 / BW2952;
RX   PubMed=19376874; DOI=10.1128/jb.00118-09;
RA   Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA   Wang L.;
RT   "Genomic sequencing reveals regulatory mutations and recombinational events
RT   in the widely used MC4100 lineage of Escherichia coli K-12.";
RL   J. Bacteriol. 191:4025-4029(2009).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001396; ACR61799.1; -; Genomic_DNA.
DR   RefSeq; WP_001216676.1; NC_012759.1.
DR   AlphaFoldDB; C4ZR77; -.
DR   SMR; C4ZR77; -.
DR   PRIDE; C4ZR77; -.
DR   GeneID; 67414819; -.
DR   KEGG; ebw:BWG_3912; -.
DR   HOGENOM; CLU_113441_6_1_6; -.
DR   OMA; ITEASPM; -.
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_1000205395"
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