ID A0A094PEB6_9ACTN Unreviewed; 89 AA.
AC A0A094PEB6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Small ribosomal subunit protein uS17 {ECO:0000256|HAMAP-Rule:MF_01345};
GN Name=rpsQ {ECO:0000256|HAMAP-Rule:MF_01345};
GN ORFNames=GM45_2605 {ECO:0000313|EMBL:KGA09317.1};
OS actinobacterium acAMD-5.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1504319 {ECO:0000313|EMBL:KGA09317.1, ECO:0000313|Proteomes:UP000029322};
RN [1] {ECO:0000313|EMBL:KGA09317.1, ECO:0000313|Proteomes:UP000029322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ghai R., Mizuno C.M., Picazo A., Camacho A., Rodriguez-Valera F.;
RT "Key roles for freshwater Actinobacteria revealed by deep metagenomic
RT sequencing.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds
CC specifically to the 5'-end of 16S ribosomal RNA. {ECO:0000256|HAMAP-
CC Rule:MF_01345}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01345}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS17 family.
CC {ECO:0000256|ARBA:ARBA00010254, ECO:0000256|HAMAP-Rule:MF_01345,
CC ECO:0000256|RuleBase:RU003872}.
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:KGA09317.1}.
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DR EMBL; JNSF01000005; KGA09317.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094PEB6; -.
DR STRING; 1504319.GM45_2605; -.
DR PATRIC; fig|1504319.4.peg.524; -.
DR eggNOG; COG0186; Bacteria.
DR Proteomes; UP000029322; 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: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 Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_01345_B; Ribosomal_S17_B; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000266; Ribosomal_uS17.
DR InterPro; IPR019984; Ribosomal_uS17_bact/chlr.
DR InterPro; IPR019979; Ribosomal_uS17_CS.
DR NCBIfam; TIGR03635; uS17_bact; 1.
DR PANTHER; PTHR10744:SF1; 37S RIBOSOMAL PROTEIN S17, MITOCHONDRIAL; 1.
DR PANTHER; PTHR10744; 40S RIBOSOMAL PROTEIN S11 FAMILY MEMBER; 1.
DR Pfam; PF00366; Ribosomal_S17; 1.
DR PRINTS; PR00973; RIBOSOMALS17.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS00056; RIBOSOMAL_S17; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01345};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01345};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01345,
KW ECO:0000256|RuleBase:RU003873};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_01345}.
SQ SEQUENCE 89 AA; 10133 MW; 58441B8DC61C4E36 CRC64;
MSKNSVERPD RKTREGLVVS DKMDKTVVVA VEDRFKHALY GKVVRRTSKL KAHDEGNTAG
IGDRVLLMET RPLSATKRWR VVEILEKAK
//