ID L0ADQ9_NATGS Unreviewed; 146 AA.
AC L0ADQ9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Small ribosomal subunit protein uS17 {ECO:0000256|HAMAP-Rule:MF_01345};
GN Name=rps17p {ECO:0000313|EMBL:ELY66621.1};
GN Synonyms=rps17 {ECO:0000256|HAMAP-Rule:MF_01345};
GN OrderedLocusNames=Natgr_0306 {ECO:0000313|EMBL:AFZ71564.1};
GN ORFNames=C490_12652 {ECO:0000313|EMBL:ELY66621.1}, CYV19_04665
GN {ECO:0000313|EMBL:PLK21333.1};
OS Natronobacterium gregoryi (strain ATCC 43098 / DSM 3393 / CCM 3738 / CIP
OS 104747 / IAM 13177 / JCM 8860 / NBRC 102187 / NCIMB 2189 / SP2).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronobacterium.
OX NCBI_TaxID=797304 {ECO:0000313|EMBL:AFZ71564.1, ECO:0000313|Proteomes:UP000010468};
RN [1] {ECO:0000313|Proteomes:UP000010468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43098 / CCM 3738 / NCIMB 2189 / SP2
RC {ECO:0000313|Proteomes:UP000010468};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA Anderson I., Woyke T.;
RT "Complete sequence of Natronobacterium gregoryi SP2.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFZ71564.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SP2 {ECO:0000313|EMBL:AFZ71564.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA Anderson I., Woyke T.;
RT "Complete sequence of Natronobacterium gregoryi SP2.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ELY66621.1, ECO:0000313|Proteomes:UP000011613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP2 {ECO:0000313|EMBL:ELY66621.1,
RC ECO:0000313|Proteomes:UP000011613};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [4] {ECO:0000313|EMBL:PLK21333.1, ECO:0000313|Proteomes:UP000234484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP2 {ECO:0000313|EMBL:PLK21333.1,
RC ECO:0000313|Proteomes:UP000234484};
RC TISSUE=Freeze-dried powder thallus {ECO:0000313|EMBL:PLK21333.1};
RA Jiang L., He B., Kang J., Yu M., Li N., Fang Y., Tang Z., Wu P., Yao P.,
RA Huang J.;
RT "The characterization of oligonucleotides binding to NgAgo.";
RL Submitted (DEC-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}.
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DR EMBL; CP003377; AFZ71564.1; -; Genomic_DNA.
DR EMBL; AOIC01000089; ELY66621.1; -; Genomic_DNA.
DR EMBL; PKKI01000009; PLK21333.1; -; Genomic_DNA.
DR RefSeq; WP_005580147.1; NZ_PKKI01000009.1.
DR AlphaFoldDB; L0ADQ9; -.
DR STRING; 797304.Natgr_0306; -.
DR GeneID; 14207470; -.
DR KEGG; nge:Natgr_0306; -.
DR PATRIC; fig|797304.7.peg.2572; -.
DR eggNOG; arCOG04096; Archaea.
DR HOGENOM; CLU_073626_0_3_2; -.
DR OMA; KKYERYE; -.
DR Proteomes; UP000010468; Chromosome.
DR Proteomes; UP000011613; Unassembled WGS sequence.
DR Proteomes; UP000234484; 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; 2.40.50.1000; -; 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 Reference proteome {ECO:0000313|Proteomes:UP000010468};
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}.
FT REGION 113..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..146
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 146 AA; 16061 MW; 06F404F61E4E6B9D CRC64;
MAIGLDVETP PEPENPEEYD YETCPFYGEL PVRGQILEGT VVSTDMDKTV VVEREYDVAV
PKYDRYMKRR SRIPAHVPGV LEPLSVGDSV KIAETRPLSK TKSHVVVEVT EEATAEDVAE
LTGQAEPEPE LSDEDLAAAA DDEGDQ
//