ID A0A1X9YBY2_9SPHN Unreviewed; 141 AA.
AC A0A1X9YBY2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Small ribosomal subunit protein bS6 {ECO:0000256|ARBA:ARBA00035294, ECO:0000256|HAMAP-Rule:MF_00360};
GN Name=rpsF {ECO:0000256|HAMAP-Rule:MF_00360};
GN ORFNames=KC8_03430 {ECO:0000313|EMBL:ARS26343.1};
OS Sphingomonas sp. KC8.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1030157 {ECO:0000313|EMBL:ARS26343.1, ECO:0000313|Proteomes:UP000194475};
RN [1] {ECO:0000313|EMBL:ARS26343.1, ECO:0000313|Proteomes:UP000194475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KC8 {ECO:0000313|EMBL:ARS26343.1};
RA Chen Y.-L., Yu C.-P., Hu A., Lee T.-H., Yang F.-C., Ismail W., Wang P.-H.,
RA Wang C.-H., Goh K.-S., Shih C.-J., Chiang Y.-R.;
RT "Bacteria use an extradiol dioxygenase-mediated pathway to degrade natural
RT estrogens in aquatic ecosystems.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds together with bS18 to 16S ribosomal RNA.
CC {ECO:0000256|ARBA:ARBA00035104, ECO:0000256|HAMAP-Rule:MF_00360}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS6 family.
CC {ECO:0000256|ARBA:ARBA00009512, ECO:0000256|HAMAP-Rule:MF_00360}.
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DR EMBL; CP016306; ARS26343.1; -; Genomic_DNA.
DR RefSeq; WP_010125006.1; NZ_CP016306.1.
DR AlphaFoldDB; A0A1X9YBY2; -.
DR STRING; 1030157.GCA_000214335_02385; -.
DR KEGG; spkc:KC8_03430; -.
DR eggNOG; COG0360; Bacteria.
DR OrthoDB; 9812702at2; -.
DR Proteomes; UP000194475; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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 CDD; cd00473; bS6; 1.
DR Gene3D; 3.30.70.60; -; 1.
DR HAMAP; MF_00360; Ribosomal_S6; 1.
DR InterPro; IPR000529; Ribosomal_bS6.
DR InterPro; IPR035980; Ribosomal_bS6_sf.
DR InterPro; IPR020814; Ribosomal_S6_plastid/chlpt.
DR InterPro; IPR014717; Transl_elong_EF1B/ribsomal_bS6.
DR NCBIfam; TIGR00166; S6; 1.
DR PANTHER; PTHR21011:SF1; 28S RIBOSOMAL PROTEIN S6, MITOCHONDRIAL; 1.
DR PANTHER; PTHR21011; MITOCHONDRIAL 28S RIBOSOMAL PROTEIN S6; 1.
DR Pfam; PF01250; Ribosomal_S6; 1.
DR SUPFAM; SSF54995; Ribosomal protein S6; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000194475};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_00360};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_00360}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_00360};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00360}.
FT REGION 97..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 141 AA; 16133 MW; 0CB72CFBB354CE41 CRC64;
MPLYEHVFLA RQDLAQAQVD ALAETATKII EEGNGKVVKT ETWGLRGIAY RIAKNRKAHY
VMIEFDAPAA VVAELERQTA INEDVIRYMT LKVDAHEAGP SAMMRRNERS ERDGRRGDRG
DRPRGDREDR PRRDRDDRDA A
//
