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Database: UniProt
Entry: A0A1G2HSF9_9BACT
LinkDB: A0A1G2HSF9_9BACT
Original site: A0A1G2HSF9_9BACT 
ID   A0A1G2HSF9_9BACT        Unreviewed;        77 AA.
AC   A0A1G2HSF9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
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=A2822_04270 {ECO:0000313|EMBL:OGZ65484.1};
OS   Candidatus Staskawiczbacteria bacterium RIFCSPHIGHO2_01_FULL_41_41.
OC   Bacteria; Candidatus Staskawiczbacteria.
OX   NCBI_TaxID=1802203 {ECO:0000313|EMBL:OGZ65484.1, ECO:0000313|Proteomes:UP000178774};
RN   [1] {ECO:0000313|EMBL:OGZ65484.1, ECO:0000313|Proteomes:UP000178774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(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   -!- 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:OGZ65484.1}.
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DR   EMBL; MHOP01000021; OGZ65484.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G2HSF9; -.
DR   Proteomes; UP000178774; 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   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.
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}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_01345};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_01345}.
SQ   SEQUENCE   77 AA;  9089 MW;  B1A6BE7F9AD7B96B CRC64;
     MSKKKLQGIV TSDKMQKTVV VEVERVTEHP KYKRRYKVHK KYKAHDENNT YKTGDTVVIE
     ETAPISKDKK WKVITKI
//
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