ID B0SSG8_LEPBP Unreviewed; 89 AA.
AC B0SSG8;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Small ribosomal subunit protein uS17 {ECO:0000256|HAMAP-Rule:MF_01345};
GN Name=rpsQ {ECO:0000256|HAMAP-Rule:MF_01345,
GN ECO:0000313|EMBL:ABZ98058.1};
GN OrderedLocusNames=LEPBI_I1955 {ECO:0000313|EMBL:ABZ98058.1};
OS Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ98058.1, ECO:0000313|Proteomes:UP000001847};
RN [1] {ECO:0000313|EMBL:ABZ98058.1, ECO:0000313|Proteomes:UP000001847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Patoc 1 / ATCC 23582 / Paris
RC {ECO:0000313|Proteomes:UP000001847};
RX PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL PLoS ONE 3:E1607-E1607(2008).
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; CP000786; ABZ98058.1; -; Genomic_DNA.
DR RefSeq; WP_012388932.1; NC_010602.1.
DR AlphaFoldDB; B0SSG8; -.
DR SMR; B0SSG8; -.
DR STRING; 456481.LEPBI_I1955; -.
DR GeneID; 50043992; -.
DR KEGG; lbi:LEPBI_I1955; -.
DR HOGENOM; CLU_073626_1_0_12; -.
DR OrthoDB; 9811714at2; -.
DR BioCyc; LBIF456481:LEPBI_RS09660-MONOMER; -.
DR Proteomes; UP000001847; Chromosome I.
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:UP000001847};
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; 10243 MW; 0EB05B56F27AB9C5 CRC64;
MEDKNSKKSL TIQGVVVSDA MDKTVVIEII TRKVHPRFKK IMTRTSRVKI HDEKNECQVG
DRVIAVETRP LSKQKHHKLV KVIEKAKLV
//
