ID E1VWA5_GLUAR Unreviewed; 86 AA.
AC E1VWA5;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
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 ECO:0000313|EMBL:CBT75908.1};
GN OrderedLocusNames=AARI_16940 {ECO:0000313|EMBL:CBT75908.1};
OS Glutamicibacter arilaitensis (strain DSM 16368 / CIP 108037 / IAM 15318 /
OS JCM 13566 / NCIMB 14258 / Re117) (Arthrobacter arilaitensis).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Glutamicibacter.
OX NCBI_TaxID=861360 {ECO:0000313|EMBL:CBT75908.1, ECO:0000313|Proteomes:UP000006878};
RN [1] {ECO:0000313|EMBL:CBT75908.1, ECO:0000313|Proteomes:UP000006878}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC {ECO:0000313|Proteomes:UP000006878};
RX PubMed=21124797; DOI=10.1371/journal.pone.0015489;
RA Monnet C., Loux V., Gibrat J.F., Spinnler E., Barbe V., Vacherie B.,
RA Gavory F., Gourbeyre E., Siguier P., Chandler M., Elleuch R., Irlinger F.,
RA Vallaeys T.;
RT "The Arthrobacter arilaitensis Re117 genome sequence reveals its genetic
RT adaptation to the surface of cheese.";
RL PLoS ONE 5:E15489-E15489(2010).
RN [2] {ECO:0000313|Proteomes:UP000006878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC {ECO:0000313|Proteomes:UP000006878};
RA Genoscope.;
RT "Complete genome sequence of Arthrobacter arilaitensis (strain DSM 16368 /
RT CIP 108037 / JCM 13566 / Re117).";
RL Submitted (JUL-2010) 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; FQ311875; CBT75908.1; -; Genomic_DNA.
DR RefSeq; WP_013349038.1; NC_014550.1.
DR AlphaFoldDB; E1VWA5; -.
DR STRING; 861360.AARI_16940; -.
DR KEGG; aai:AARI_16940; -.
DR eggNOG; COG0268; Bacteria.
DR HOGENOM; CLU_160655_0_1_11; -.
DR OrthoDB; 9807974at2; -.
DR Proteomes; UP000006878; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000006878};
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 COILED 2..29
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 86 AA; 9404 MW; 37AD7F9B9D86B591 CRC64;
MANIKSQKKR NLTNEKARLR NVAVRSEVKT VIRNVNEAVV SGDKEKATEA LRLAGKKLDK
AVSKGVLHKN NAANRKSAIA KKVNAL
//
