ID A4TEB5_MYCGI Unreviewed; 98 AA.
AC A4TEB5;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
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=Mflv_5040 {ECO:0000313|EMBL:ABP47506.1};
OS Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS PYR-GCK)).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350054 {ECO:0000313|EMBL:ABP47506.1};
RN [1] {ECO:0000313|EMBL:ABP47506.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP47506.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABP47506.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP47506.1};
RX PubMed=23469141;
RA Badejo A.C., Badejo A.O., Shin K.H., Chai Y.G.;
RT "A Gene Expression Study of the Activities of Aromatic Ring-Cleavage
RT Dioxygenases in Mycobacterium gilvum PYR-GCK to Changes in Salinity and pH
RT during Pyrene Degradation.";
RL PLoS ONE 8:E58066-E58066(2013).
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}.
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DR EMBL; CP000656; ABP47506.1; -; Genomic_DNA.
DR AlphaFoldDB; A4TEB5; -.
DR STRING; 350054.Mflv_5040; -.
DR KEGG; mgi:Mflv_5040; -.
DR eggNOG; COG0186; Bacteria.
DR HOGENOM; CLU_073626_1_0_11; -.
DR OrthoDB; 9811714at2; -.
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 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.
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}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_01345};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_01345}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 98 AA; 11163 MW; BA3EC74ADE82D9DC CRC64;
MADTKGEKHT PRTEDKRGRR KTAIGYVVSD KMQKTIVVEL ESRKSHPLYG KIIRTTTKVK
AHDENESAGI GDRVSLMETR PTSATKRWRL VEVLEKAK
//