ID   B0RB48_CLASE            Unreviewed;       100 AA.
AC   B0RB48;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   02-SEP-2026, entry version 114.
DE   RecName: Full=Small ribosomal subunit protein uS17 {ECO:0000256|HAMAP-Rule:MF_01345};
GN   Name=rpsQ {ECO:0000256|HAMAP-Rule:MF_01345};
GN   OrderedLocusNames=CMS0292 {ECO:0000313|EMBL:CAQ00413.1};
OS   Clavibacter sepedonicus (Clavibacter michiganensis subsp. sepedonicus).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Microbacteriaceae; Clavibacter.
OX   NCBI_TaxID=31964 {ECO:0000313|EMBL:CAQ00413.1, ECO:0000313|Proteomes:UP000001318};
RN   [1] {ECO:0000313|EMBL:CAQ00413.1, ECO:0000313|Proteomes:UP000001318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / ICMP 2535 / C-1
RC   {ECO:0000313|Proteomes:UP000001318};
RX   PubMed=18192393; DOI=10.1128/JB.01598-07;
RA   Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA   Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA   Parkhill J., Ishimaru C.A.;
RT   "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp.
RT   sepedonicus suggests recent niche adaptation.";
RL   J. Bacteriol. 190:2150-2160(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.
CC       {ECO:0000256|ARBA:ARBA00011458, ECO:0000256|HAMAP-Rule:MF_01345}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS17 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01345, ECO:0000256|RuleBase:RU003872}.
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DR   EMBL; AM849034; CAQ00413.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0RB48; -.
DR   STRING; 31964.CMS0292; -.
DR   KEGG; cms:CMS0292; -.
DR   eggNOG; COG0186; Bacteria.
DR   HOGENOM; CLU_073626_1_0_11; -.
DR   Proteomes; UP000001318; Chromosome.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IEA:UniProtKB-UniRule.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00364; Ribosomal_uS17; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   HAMAP; MF_01345_B; Ribosomal_uS17_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; NF004123; PRK05610.1; 1.
DR   NCBIfam; TIGR03635; uS17_bact; 1.
DR   PANTHER; PTHR10744; 40S RIBOSOMAL PROTEIN S11 FAMILY MEMBER; 1.
DR   PANTHER; PTHR10744:SF1; SMALL RIBOSOMAL SUBUNIT PROTEIN US17M; 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:UP000001318};
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|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01345};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_01345}.
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..11
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   100 AA;  11313 MW;  F6A822FA25ACB5D1 CRC64;
     MIMANAEEKN TADTATADRG YRKSRRGYVT SDKMDKTIVV EVEDRVKHPL YGKVIRRTSK
     VKAHDEANTA GIGDLVLINE TRPLSASKRW RLVEILEKAK
//