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Database: UniProt
Entry: I3YWM2_AEQSU
LinkDB: I3YWM2_AEQSU
Original site: I3YWM2_AEQSU 
ID   I3YWM2_AEQSU            Unreviewed;        87 AA.
AC   I3YWM2;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 51.
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=Aeqsu_1916 {ECO:0000313|EMBL:AFL81390.1};
OS   Aequorivita sublithincola (strain DSM 14238 / LMG 21431 / ACAM 643 / 9-3).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Aequorivita.
OX   NCBI_TaxID=746697 {ECO:0000313|EMBL:AFL81390.1, ECO:0000313|Proteomes:UP000006049};
RN   [1] {ECO:0000313|EMBL:AFL81390.1, ECO:0000313|Proteomes:UP000006049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14238 / LMG 21431 / ACAM 643 / 9-3
RC   {ECO:0000313|Proteomes:UP000006049};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA   Munk A.C.C., Kyrpides N., Mavromatis K., Pagani I., Ivanova N.,
RA   Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA   Faehnrich R., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Aequorivita sublithincola DSM 14238.";
RL   Submitted (JUN-2012) 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; CP003280; AFL81390.1; -; Genomic_DNA.
DR   RefSeq; WP_014782644.1; NC_018013.1.
DR   AlphaFoldDB; I3YWM2; -.
DR   STRING; 746697.Aeqsu_1916; -.
DR   KEGG; asl:Aeqsu_1916; -.
DR   PATRIC; fig|746697.3.peg.1950; -.
DR   eggNOG; COG0186; Bacteria.
DR   HOGENOM; CLU_073626_1_0_10; -.
DR   OrthoDB; 9811714at2; -.
DR   Proteomes; UP000006049; 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   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   87 AA;  10190 MW;  F3DA30A607201C4F CRC64;
     MEEIKRNLRK ERIGVVTSNK MDKSIVVAEV KKVKHPMYGK FVLKTKKYVA HDETNNCNEG
     DTVKIMETRP LSKTKCWRLV EIIERAK
//
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