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Database: UniProt
Entry: A0A1M3F8C3_9CELL
LinkDB: A0A1M3F8C3_9CELL
Original site: A0A1M3F8C3_9CELL 
ID   A0A1M3F8C3_9CELL        Unreviewed;        97 AA.
AC   A0A1M3F8C3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=BGO37_15485 {ECO:0000313|EMBL:OJV80924.1};
OS   Cellulomonas sp. 73-92.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1895740 {ECO:0000313|EMBL:OJV80924.1, ECO:0000313|Proteomes:UP000184539};
RN   [1] {ECO:0000313|EMBL:OJV80924.1, ECO:0000313|Proteomes:UP000184539}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=73-92 {ECO:0000313|EMBL:OJV80924.1};
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|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}.
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:OJV80924.1}.
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DR   EMBL; MKTH01000013; OJV80924.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3F8C3; -.
DR   STRING; 1895740.BGO37_15485; -.
DR   Proteomes; UP000184539; 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; IPR020815; Ribosomal_bS6_CS.
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.
DR   PROSITE; PS01048; RIBOSOMAL_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:OJV80924.1};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00360};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_00360}.
SQ   SEQUENCE   97 AA;  11011 MW;  252A811E4F49DA8A CRC64;
     MSLRQYEIMI ILDPEIEERT VAPSLDKYLT VVKSDGGSVD KVDIWGRRRL AYDIKKKAEG
     IYAVVNFTAE PATAKELDRQ LGLNEVVLRT KVLRTDS
//
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