ID A0A0B0DJM3_9MICC Unreviewed; 95 AA.
AC A0A0B0DJM3;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=AS25_00895 {ECO:0000313|EMBL:KHE75419.1};
OS Kocuria marina.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=223184 {ECO:0000313|EMBL:KHE75419.1, ECO:0000313|Proteomes:UP000030664};
RN [1] {ECO:0000313|EMBL:KHE75419.1, ECO:0000313|Proteomes:UP000030664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO9-6 {ECO:0000313|EMBL:KHE75419.1,
RC ECO:0000313|Proteomes:UP000030664};
RA Castro D.B., Pereira L.B., Silva M.V., Silva B.P., Zanardi B.R., Carlos C.,
RA Belgini D.R., Limache E.G., Lacerda G.V., Nery M.B., Gomes M.B., Souza S.,
RA Silva T.M., Rodrigues V.D., Paulino L.C., Vicentini R., Ferraz L.F.,
RA Ottoboni L.M.;
RT "High-quality draft genome sequence of Kocuria marina SO9-6, an
RT actinobacterium isolated from a copper mine.";
RL Submitted (SEP-2014) 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}.
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:KHE75419.1}.
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DR EMBL; JROM01000007; KHE75419.1; -; Genomic_DNA.
DR RefSeq; WP_035959699.1; NZ_JROM01000007.1.
DR AlphaFoldDB; A0A0B0DJM3; -.
DR STRING; 223184.AS25_00895; -.
DR GeneID; 85730213; -.
DR eggNOG; COG0186; Bacteria.
DR Proteomes; UP000030664; 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 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 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}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 95 AA; 10764 MW; 3051AD3586839036 CRC64;
MSEQVNNESA AAERGDRKTR QGYVVSDKMD KTVVVQVEDR VKHALYGKVL RKSKRVKAHD
EQNTCGVGDL VRIAETRPLS ATKNWRIVEI IEKAK
//
