ID   RS6_ECO81               Reviewed;         131 AA.
AC   B7MST0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=30S ribosomal protein S6 {ECO:0000255|HAMAP-Rule:MF_00360};
GN   Name=rpsF {ECO:0000255|HAMAP-Rule:MF_00360}; OrderedLocusNames=ECED1_5050;
OS   Escherichia coli O81 (strain ED1a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ED1a;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(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}.
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DR   EMBL; CU928162; CAR11005.1; -; Genomic_DNA.
DR   RefSeq; WP_001216676.1; NC_011745.1.
DR   AlphaFoldDB; B7MST0; -.
DR   SMR; B7MST0; -.
DR   EnsemblBacteria; CAR11005; CAR11005; ECED1_5050.
DR   GeneID; 67414819; -.
DR   KEGG; ecq:ECED1_5050; -.
DR   HOGENOM; CLU_113441_6_1_6; -.
DR   OMA; ITEASPM; -.
DR   Proteomes; UP000000748; 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_1000133529"
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