ID A0A3N8MU77_9BURK Unreviewed; 266 AA.
AC A0A3N8MU77;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=DID96_10600 {ECO:0000313|EMBL:RQS72202.1};
OS Burkholderia sp. Bp8963.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=2184547 {ECO:0000313|EMBL:RQS72202.1, ECO:0000313|Proteomes:UP000274808};
RN [1] {ECO:0000313|EMBL:RQS72202.1, ECO:0000313|Proteomes:UP000274808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp8963 {ECO:0000313|EMBL:RQS72202.1,
RC ECO:0000313|Proteomes:UP000274808};
RA Hall C., Sahl J., Wagner D.;
RT "Comparative analysis of Burkholderia isolates from Puerto Rico.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RQS72202.1}.
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DR EMBL; QTQP01000010; RQS72202.1; -; Genomic_DNA.
DR RefSeq; WP_006400654.1; NZ_QTQP01000010.1.
DR AlphaFoldDB; A0A3N8MU77; -.
DR SMR; A0A3N8MU77; -.
DR GeneID; 66525182; -.
DR OrthoDB; 9806396at2; -.
DR Proteomes; UP000274808; Unassembled WGS sequence.
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:UP000274808};
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 39..107
FT /note="KH type-2"
FT /evidence="ECO:0000259|PROSITE:PS50823"
FT REGION 218..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 266 AA; 29903 MW; 598E1519A53E6C24 CRC64;
MGQKIHPTGF RLAVSRNWAS RWYANNNNFA AMLQEDIGVR EYLKKKLKNA SVGRVVIERP
AKNARITIFS SRPGVVIGKK GEDIELLKTE LQRRMGVPVH VNIEEIRKPE TDAQLIADSI
TQQLERRIMF RRAMKRAMQN AMRLGAQGIK IMSAGRLNGI EIARTEWYRE GRVPLHTLRA
DIDYATSEAK TTYGIIGVKV WVYKGDTLGR NDAPVVEEVA EDKRPRRNAR PGDRRPRRDG
EGGAPGARRG APRRGAGKPE DGKTGE
//
