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Database: UniProt
Entry: A0A1Y2K4I3_9PROT
LinkDB: A0A1Y2K4I3_9PROT
Original site: A0A1Y2K4I3_9PROT 
ID   A0A1Y2K4I3_9PROT        Unreviewed;       132 AA.
AC   A0A1Y2K4I3;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=MAIT1_02754 {ECO:0000313|EMBL:OSM02577.1};
OS   Magnetofaba australis IT-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Magnetococcales;
OC   Magnetococcaceae; Magnetofaba.
OX   NCBI_TaxID=1434232 {ECO:0000313|EMBL:OSM02577.1, ECO:0000313|Proteomes:UP000194003};
RN   [1] {ECO:0000313|EMBL:OSM02577.1, ECO:0000313|Proteomes:UP000194003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IT-1 {ECO:0000313|EMBL:OSM02577.1,
RC   ECO:0000313|Proteomes:UP000194003};
RX   PubMed=27801294; DOI=10.1186/s12864-016-3064-9;
RA   Araujo A.C., Morillo V., Cypriano J., Teixeira L.C., Leao P., Lyra S.,
RA   Almeida L.G., Bazylinski D.A., Vasconcellos A.T., Abreu F., Lins U.;
RT   "Combined genomic and structural analyses of a cultured magnetotactic
RT   bacterium reveals its niche adaptation to a dynamic environment.";
RL   BMC Genomics 17:726-726(2016).
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:OSM02577.1}.
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DR   EMBL; LVJN01000020; OSM02577.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2K4I3; -.
DR   STRING; 1434232.MAIT1_02754; -.
DR   OrthoDB; 9812702at2; -.
DR   Proteomes; UP000194003; 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   Reference proteome {ECO:0000313|Proteomes:UP000194003};
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..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..132
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   132 AA;  14990 MW;  67BB2B778FCD63E9 CRC64;
     MAFYETIYIL RPDLSNEQVE QVVKRVGEMI EGLGGKILKT EMWGRRQLAY LVKKNNKGFY
     VFHSVEGGGT LVHELESKLR IDEDVIKFQN IRVEQAFADP TPLAPQEEPK SEEKGDEAEA
     SEETTEATAD EE
//
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