ID A0A0G3H4G4_9CORY Unreviewed; 87 AA.
AC A0A0G3H4G4;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Small ribosomal subunit protein bS20 {ECO:0000256|ARBA:ARBA00035136, ECO:0000256|HAMAP-Rule:MF_00500};
GN Name=rpsT {ECO:0000256|HAMAP-Rule:MF_00500};
GN ORFNames=CMUST_11985 {ECO:0000313|EMBL:AKK06708.1};
OS Corynebacterium mustelae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=571915 {ECO:0000313|EMBL:AKK06708.1, ECO:0000313|Proteomes:UP000035199};
RN [1] {ECO:0000313|EMBL:AKK06708.1, ECO:0000313|Proteomes:UP000035199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45274 {ECO:0000313|EMBL:AKK06708.1,
RC ECO:0000313|Proteomes:UP000035199};
RX PubMed=26358597;
RA Ruckert C., Eimer J., Winkler A., Tauch A.;
RT "Complete Genome Sequence of the Type Strain Corynebacterium mustelae DSM
RT 45274, Isolated from Various Tissues of a Male Ferret with Lethal Sepsis.";
RL Genome Announc. 3:e01012-15(2015).
RN [2] {ECO:0000313|Proteomes:UP000035199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45274 {ECO:0000313|Proteomes:UP000035199};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium mustelae DSM 45274, isolated
RT from various tissues of a male ferret with lethal sepsis.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds directly to 16S ribosomal RNA. {ECO:0000256|HAMAP-
CC Rule:MF_00500}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS20 family.
CC {ECO:0000256|ARBA:ARBA00007634, ECO:0000256|HAMAP-Rule:MF_00500}.
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DR EMBL; CP011542; AKK06708.1; -; Genomic_DNA.
DR RefSeq; WP_047262685.1; NZ_CP011542.1.
DR AlphaFoldDB; A0A0G3H4G4; -.
DR STRING; 571915.CMUST_11985; -.
DR KEGG; cmv:CMUST_11985; -.
DR PATRIC; fig|571915.4.peg.2559; -.
DR OrthoDB; 9807974at2; -.
DR Proteomes; UP000035199; 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; 1.20.58.110; Ribosomal protein S20; 1.
DR HAMAP; MF_00500; Ribosomal_S20; 1.
DR InterPro; IPR002583; Ribosomal_bS20.
DR InterPro; IPR036510; Ribosomal_bS20_sf.
DR NCBIfam; TIGR00029; S20; 1.
DR PANTHER; PTHR33398; 30S RIBOSOMAL PROTEIN S20; 1.
DR PANTHER; PTHR33398:SF1; 30S RIBOSOMAL PROTEIN S20, CHLOROPLASTIC; 1.
DR Pfam; PF01649; Ribosomal_S20p; 1.
DR SUPFAM; SSF46992; Ribosomal protein S20; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000035199};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_00500};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_00500};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00500};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_00500}.
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 87 AA; 9805 MW; 419B463C7D584872 CRC64;
MANIKSQKKR VLTNEKRRQR NQAVRSAVRT EIRKFRELVA EGDKAAAEAQ LRVASRALDK
SVTKGVFHRN NAANKKSKMA NALNKMA
//
