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Database: UniProt
Entry: G2ND65_STREK
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ID   G2ND65_STREK            Unreviewed;       278 AA.
AC   G2ND65;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Small ribosomal subunit protein uS3 {ECO:0000256|ARBA:ARBA00035257, ECO:0000256|HAMAP-Rule:MF_01309};
GN   Name=rpsC {ECO:0000256|HAMAP-Rule:MF_01309};
GN   ORFNames=SACTE_3974 {ECO:0000313|EMBL:AEN11817.1};
OS   Streptomyces sp. (strain SirexAA-E / ActE).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN11817.1, ECO:0000313|Proteomes:UP000001397};
RN   [1] {ECO:0000313|EMBL:AEN11817.1, ECO:0000313|Proteomes:UP000001397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A., Raffa K.,
RA   Adams S., Book A., Currie C., Woyke T.;
RT   "Complete sequence of Streptomyces sp. SirexAA-E.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEN11817.1, ECO:0000313|Proteomes:UP000001397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RX   PubMed=24710170; DOI=10.1371/journal.pone.0094166;
RA   Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F.,
RA   Book A.J., Currie C.R., Fox B.G.;
RT   "Biochemical properties and atomic resolution structure of a
RT   proteolytically processed beta-mannanase from cellulolytic Streptomyces sp.
RT   SirexAA-E.";
RL   PLoS ONE 9:e94166-E94166(2014).
CC   -!- FUNCTION: Binds the lower part of the 30S subunit head. Binds mRNA in
CC       the 70S ribosome, positioning it for translation.
CC       {ECO:0000256|ARBA:ARBA00024998, ECO:0000256|HAMAP-Rule:MF_01309}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a tight complex with
CC       proteins S10 and S14. {ECO:0000256|HAMAP-Rule:MF_01309}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS3 family.
CC       {ECO:0000256|ARBA:ARBA00010761, ECO:0000256|HAMAP-Rule:MF_01309,
CC       ECO:0000256|RuleBase:RU003624}.
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DR   EMBL; CP002993; AEN11817.1; -; Genomic_DNA.
DR   RefSeq; WP_014047784.1; NC_015953.1.
DR   AlphaFoldDB; G2ND65; -.
DR   STRING; 862751.SACTE_3974; -.
DR   KEGG; ssx:SACTE_3974; -.
DR   PATRIC; fig|862751.12.peg.4125; -.
DR   eggNOG; COG0092; Bacteria.
DR   HOGENOM; CLU_058591_0_0_11; -.
DR   OrthoDB; 9806396at2; -.
DR   Proteomes; UP000001397; Chromosome.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; IEA:UniProtKB-UniRule.
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; cd02412; KH-II_30S_S3; 1.
DR   Gene3D; 3.30.300.20; -; 1.
DR   Gene3D; 3.30.1140.32; Ribosomal protein S3, C-terminal domain; 1.
DR   HAMAP; MF_01309_B; Ribosomal_S3_B; 1.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR015946; KH_dom-like_a/b.
DR   InterPro; IPR004044; KH_dom_type_2.
DR   InterPro; IPR009019; KH_sf_prok-type.
DR   InterPro; IPR036419; Ribosomal_S3_C_sf.
DR   InterPro; IPR005704; Ribosomal_uS3_bac-typ.
DR   InterPro; IPR001351; Ribosomal_uS3_C.
DR   InterPro; IPR018280; Ribosomal_uS3_CS.
DR   NCBIfam; TIGR01009; rpsC_bact; 1.
DR   PANTHER; PTHR11760:SF19; 30S RIBOSOMAL PROTEIN S3, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR11760; 30S/40S RIBOSOMAL PROTEIN S3; 1.
DR   Pfam; PF07650; KH_2; 1.
DR   Pfam; PF00189; Ribosomal_S3_C; 1.
DR   SMART; SM00322; KH; 1.
DR   SUPFAM; SSF54814; Prokaryotic type KH domain (KH-domain type II); 1.
DR   SUPFAM; SSF54821; Ribosomal protein S3 C-terminal domain; 1.
DR   PROSITE; PS50823; KH_TYPE_2; 1.
DR   PROSITE; PS00548; RIBOSOMAL_S3; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001397};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_01309};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_01309};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01309};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_01309}.
FT   DOMAIN          38..106
FT                   /note="KH type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50823"
FT   REGION          216..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   278 AA;  30346 MW;  B8937B1B818D91FA CRC64;
     MGQKVNPHGF RLGITTDFKS RWYADKLYKD YVKEDVAIRR MMTKGMERAG ISKVEIERTR
     DRVRVDIHTA RPGIVIGRRG AEADRIRGEL EKLTGKQVQL NILEVKNPEV DAQLVAQAVA
     EQLSSRVSFR RAMRKSMQST MKAGAKGIKI QCGGRLGGAE MSRSEFYREG RVPLHTLRAN
     VDYGFFEAKT TFGRIGVKVW IYKGDVKNIA EVRAENAAAR AGNRPARGGA DRPAGRGGRG
     GERGGRGRKP QQSAPAAEAP KADAPAAAAP AESTGTEA
//
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