ID A0A1Q5L264_9ACTN Unreviewed; 103 AA.
AC A0A1Q5L264;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=AMK31_12440 {ECO:0000313|EMBL:OKJ87933.1};
OS Streptomyces sp. TSRI0107.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703942 {ECO:0000313|EMBL:OKJ87933.1, ECO:0000313|Proteomes:UP000185813};
RN [1] {ECO:0000313|EMBL:OKJ87933.1, ECO:0000313|Proteomes:UP000185813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSRI0107 {ECO:0000313|EMBL:OKJ87933.1,
RC ECO:0000313|Proteomes:UP000185813};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKJ87933.1}.
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DR EMBL; LIVZ01000004; OKJ87933.1; -; Genomic_DNA.
DR RefSeq; WP_073940531.1; NZ_LIVZ01000004.1.
DR AlphaFoldDB; A0A1Q5L264; -.
DR STRING; 1703942.AMK31_12440; -.
DR OrthoDB; 9811714at2; -.
DR Proteomes; UP000185813; 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 Reference proteome {ECO:0000313|Proteomes:UP000185813};
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}.
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 103 AA; 11363 MW; 5017F2E15F79B1B0 CRC64;
MSENNVTEQT AGTSGSAAGE ARGFRKTREG LVVSDKMDKT VVVAVEDRVK HALYGKVIRR
TNKLKAHDEQ NAAGVGDRVL LMETRPLSAT KRWRVVEILE KAK
//
