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Database: UniProt
Entry: A0A1G2HMN1_9BACT
LinkDB: A0A1G2HMN1_9BACT
Original site: A0A1G2HMN1_9BACT 
ID   A0A1G2HMN1_9BACT        Unreviewed;       148 AA.
AC   A0A1G2HMN1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   08-NOV-2023, entry version 19.
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=A2730_00685 {ECO:0000313|EMBL:OGZ63792.1};
OS   Candidatus Staskawiczbacteria bacterium RIFCSPHIGHO2_01_FULL_39_25.
OC   Bacteria; Candidatus Staskawiczbacteria.
OX   NCBI_TaxID=1802202 {ECO:0000313|EMBL:OGZ63792.1, ECO:0000313|Proteomes:UP000176855};
RN   [1] {ECO:0000313|EMBL:OGZ63792.1, ECO:0000313|Proteomes:UP000176855}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGZ63792.1}.
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DR   EMBL; MHOO01000011; OGZ63792.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G2HMN1; -.
DR   STRING; 1802202.A2730_00685; -.
DR   Proteomes; UP000176855; Unassembled WGS sequence.
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:OGZ63792.1};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00360};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00360}.
FT   REGION          101..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   148 AA;  16806 MW;  D33B09F1AA3BB7BA CRC64;
     MKSYELTYII SSSASSEQME GTIKEIETFI QGKGGVILRS EKTSAQTLAY PIKKHSSGYF
     VILTFQTAED TIKPIKERVE KDQQILRSFI LVKKPAKEMK ERRTRKPFVA PESDALASPV
     PKFTEDKHKG EKVKAEEIDK KLEEILGE
//
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