ID   RS5_STRCO               Reviewed;         201 AA.
AC   P46790; Q9L0C3;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   18-OCT-2001, sequence version 3.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=30S ribosomal protein S5 {ECO:0000255|HAMAP-Rule:MF_01307};
GN   Name=rpsE {ECO:0000255|HAMAP-Rule:MF_01307}; OrderedLocusNames=SCO4719;
GN   ORFNames=SCD31.44;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A3(2) / NRRL B-16638;
RA   Loriaux A., Brans A., Dusart J.;
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- FUNCTION: With S4 and S12 plays an important role in translational
CC       accuracy. {ECO:0000255|HAMAP-Rule:MF_01307}.
CC   -!- FUNCTION: Located at the back of the 30S subunit body where it
CC       stabilizes the conformation of the head with respect to the body.
CC       {ECO:0000255|HAMAP-Rule:MF_01307}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S4 and
CC       S8. {ECO:0000255|HAMAP-Rule:MF_01307}.
CC   -!- DOMAIN: The N-terminal domain interacts with the head of the 30S
CC       subunit; the C-terminal domain interacts with the body and contacts
CC       protein S4. The interaction surface between S4 and S5 is involved in
CC       control of translational fidelity.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01307}.
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; X83011; CAA58136.1; -; Genomic_DNA.
DR   EMBL; AL939121; CAB82087.1; -; Genomic_DNA.
DR   PIR; S50003; S50003.
DR   RefSeq; NP_628878.1; NC_003888.3.
DR   RefSeq; WP_003974251.1; NZ_VNID01000016.1.
DR   AlphaFoldDB; P46790; -.
DR   SMR; P46790; -.
DR   STRING; 100226.SCO4719; -.
DR   GeneID; 1100160; -.
DR   KEGG; sco:SCO4719; -.
DR   PATRIC; fig|100226.15.peg.4790; -.
DR   eggNOG; COG0098; Bacteria.
DR   HOGENOM; CLU_065898_1_2_11; -.
DR   InParanoid; P46790; -.
DR   OMA; KRGCGSW; -.
DR   PhylomeDB; P46790; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IBA:GO_Central.
DR   Gene3D; 3.30.230.10; -; 1.
DR   HAMAP; MF_01307_B; Ribosomal_S5_B; 1.
DR   InterPro; IPR000851; Ribosomal_S5.
DR   InterPro; IPR005712; Ribosomal_S5_bac-type.
DR   InterPro; IPR005324; Ribosomal_S5_C.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR013810; Ribosomal_S5_N.
DR   InterPro; IPR018192; Ribosomal_S5_N_CS.
DR   PANTHER; PTHR13718; PTHR13718; 1.
DR   Pfam; PF00333; Ribosomal_S5; 1.
DR   Pfam; PF03719; Ribosomal_S5_C; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   TIGRFAMs; TIGR01021; rpsE_bact; 1.
DR   PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR   PROSITE; PS50881; S5_DSRBD; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..201
FT                   /note="30S ribosomal protein S5"
FT                   /id="PRO_0000131604"
FT   DOMAIN          34..97
FT                   /note="S5 DRBM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01307"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        9..10
FT                   /note="SG -> RR (in Ref. 1; CAA58136)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        84
FT                   /note="A -> V (in Ref. 1; CAA58136)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   201 AA;  20500 MW;  FFDD4F35A12081E9 CRC64;
     MAGPQRRGSG AGGGERRDRK GRDGGAGAAE KTAYVERVVA INRVAKVVKG GRRFSFTALV
     VVGDGDGTVG VGYGKAKEVP AAIAKGVEEA KKHFFKVPRI QGTIPHPIQG EKAAGVVLLK
     PASPGTGVIA GGPVRAVLEC AGIHDVLSKS LGSDNQINIV HATVEALKGL QRPEEIAARR
     GLPLEDVAPA ALLRARAGAG A