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Database: UniProt
Entry: F5X455_STRPX
LinkDB: F5X455_STRPX
Original site: F5X455_STRPX 
ID   F5X455_STRPX            Unreviewed;        86 AA.
AC   F5X455;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 70.
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:BAK29195.1};
GN   OrderedLocusNames=SGPB_0057 {ECO:0000313|EMBL:BAK29195.1};
OS   Streptococcus pasteurianus (strain ATCC 43144 / JCM 5346 / CDC 1723-81).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=981540 {ECO:0000313|EMBL:BAK29195.1, ECO:0000313|Proteomes:UP000007946};
RN   [1] {ECO:0000313|EMBL:BAK29195.1, ECO:0000313|Proteomes:UP000007946}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43144 / JCM 5346 / CDC 1723-81
RC   {ECO:0000313|Proteomes:UP000007946};
RX   PubMed=21633709; DOI=10.1371/journal.pone.0020519;
RA   Lin I.-H., Liu T.-T., Teng Y.-T., Wu H.-L., Liu Y.-M., Wu K.-M.,
RA   Chang C.-H., Hsu M.-T.;
RT   "Sequencing and comparative genome analysis of two pathogenic Streptococcus
RT   gallolyticus subspecies: genome plasticity, adaptation and virulence.";
RL   PLoS ONE 6:E20519-E20519(2011).
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; AP012054; BAK29195.1; -; Genomic_DNA.
DR   RefSeq; WP_002885836.1; NC_015600.1.
DR   AlphaFoldDB; F5X455; -.
DR   SMR; F5X455; -.
DR   STRING; 981540.SGPB_0057; -.
DR   GeneID; 69902744; -.
DR   KEGG; stb:SGPB_0057; -.
DR   HOGENOM; CLU_073626_1_0_9; -.
DR   Proteomes; UP000007946; Chromosome.
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:UP000007946};
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   86 AA;  10027 MW;  E5000FF7703D1FE1 CRC64;
     MERNQRKTLV GRVVSDKMDK TITVVVETKR NHPVYGKRIN YSKKYKAHDE NNVAKEGDIV
     RIMETRPLSA TKRFRLVEVV EEAVII
//
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