ID A0A2H9HZS6_9ARCH Unreviewed; 112 AA.
AC A0A2H9HZS6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Small ribosomal subunit protein uS17 {ECO:0000256|HAMAP-Rule:MF_01345};
GN Name=rps17 {ECO:0000256|HAMAP-Rule:MF_01345};
GN ORFNames=CP083_02845 {ECO:0000313|EMBL:PDM26631.1};
OS Candidatus Bathyarchaeota archaeon B24-2.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=2041147 {ECO:0000313|EMBL:PDM26631.1, ECO:0000313|Proteomes:UP000228824};
RN [1] {ECO:0000313|EMBL:PDM26631.1, ECO:0000313|Proteomes:UP000228824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B24-2 {ECO:0000313|EMBL:PDM26631.1};
RA Feng X., Perumal V., Wang F.;
RT "Metabolic analysis of an uncultured genome Bathyarchaeota B242 based on
RT metagenomic technology.";
RL Submitted (SEP-2017) 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:PDM26631.1}.
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DR EMBL; PCNA01000018; PDM26631.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H9HZS6; -.
DR Proteomes; UP000228824; Unassembled WGS sequence.
DR GO; GO:0022626; C:cytosolic ribosome; IEA:UniProt.
DR GO; GO:1990904; C:ribonucleoprotein complex; 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; 2.40.50.1000; -; 1.
DR HAMAP; MF_01345_A; Ribosomal_S17_A; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000266; Ribosomal_uS17.
DR InterPro; IPR028333; Ribosomal_uS17_arc/euk.
DR InterPro; IPR019978; Ribosomal_uS17_archaeal.
DR InterPro; IPR019979; Ribosomal_uS17_CS.
DR NCBIfam; TIGR03630; uS17_arch; 1.
DR PANTHER; PTHR10744:SF9; 40S RIBOSOMAL PROTEIN S11; 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|HAMAP-Rule:MF_01345,
KW ECO:0000256|RuleBase:RU003872};
KW Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_01345,
KW ECO:0000256|RuleBase:RU003872};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01345};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01345}.
SQ SEQUENCE 112 AA; 12724 MW; 4855F20B08D0B59B CRC64;
MPAITLKKPK ASCNDVNCPF HGKLSVRGKV LEGVVVSDKM DKTVIVRRDY LHYVPKYMRY
ERRHSRIPAH NPPCINAKMG DKVRIMECRP ISKTVSFVVV EKLEEEKGGG QS
//