ID A0A1Q3QWC6_9BACT Unreviewed; 161 AA.
AC A0A1Q3QWC6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=BGO25_13455 {ECO:0000313|EMBL:OJV44104.1};
OS Acidobacteriales bacterium 59-55.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales.
OX NCBI_TaxID=1895690 {ECO:0000313|EMBL:OJV44104.1, ECO:0000313|Proteomes:UP000186822};
RN [1] {ECO:0000313|EMBL:OJV44104.1, ECO:0000313|Proteomes:UP000186822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=59-55 {ECO:0000313|EMBL:OJV44104.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds together with bS18 to 16S ribosomal RNA.
CC {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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJV44104.1}.
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DR EMBL; MKSV01000003; OJV44104.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3QWC6; -.
DR STRING; 1895690.BGO25_13455; -.
DR Proteomes; UP000186822; Unassembled WGS sequence.
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 Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_00360};
KW Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_00360,
KW ECO:0000313|EMBL:OJV44104.1};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00360};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00360}.
FT REGION 118..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 161 AA; 17407 MW; C1CAB1E3A17E3955 CRC64;
MNRTYEIMFI VRPDVEEAEI DKLIEGFSAN VTSGGGEVKS VEKMGRRRLA YTVRKFNDGF
YVLLNIAAEG SLITEIERRL RVSEQVIKFI TVRMDEEEKR LAKVKALRDS KVKRSALPVA
QPAAATETEA PAAAKEAPAA APTATPETAA PAASSEAAAA V
//