ID A0A085FQA0_9BURK Unreviewed; 131 AA.
AC A0A085FQA0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Small ribosomal subunit protein uS8 {ECO:0000256|ARBA:ARBA00035258, ECO:0000256|HAMAP-Rule:MF_01302};
GN Name=rpsH {ECO:0000256|HAMAP-Rule:MF_01302,
GN ECO:0000313|EMBL:KFC73645.1};
GN ORFNames=FG94_01424 {ECO:0000313|EMBL:KFC73645.1};
OS Massilia sp. LC238.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1502852 {ECO:0000313|EMBL:KFC73645.1, ECO:0000313|Proteomes:UP000028601};
RN [1] {ECO:0000313|EMBL:KFC73645.1, ECO:0000313|Proteomes:UP000028601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC238 {ECO:0000313|EMBL:KFC73645.1,
RC ECO:0000313|Proteomes:UP000028601};
RA Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT isolate.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC to 16S rRNA central domain where it helps coordinate assembly of the
CC platform of the 30S subunit. {ECO:0000256|HAMAP-Rule:MF_01302}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S5 and
CC S12. {ECO:0000256|HAMAP-Rule:MF_01302}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS8 family.
CC {ECO:0000256|ARBA:ARBA00006471, ECO:0000256|HAMAP-Rule:MF_01302,
CC ECO:0000256|RuleBase:RU003660}.
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:KFC73645.1}.
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DR EMBL; JNNN01000030; KFC73645.1; -; Genomic_DNA.
DR RefSeq; WP_027867250.1; NZ_JNNN01000030.1.
DR AlphaFoldDB; A0A085FQA0; -.
DR STRING; 1502852.FG94_01424; -.
DR PATRIC; fig|1502852.3.peg.1400; -.
DR eggNOG; COG0096; Bacteria.
DR OrthoDB; 9802617at2; -.
DR Proteomes; UP000028601; 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 Gene3D; 3.30.1370.30; -; 1.
DR Gene3D; 3.30.1490.10; -; 1.
DR HAMAP; MF_01302_B; Ribosomal_S8_B; 1.
DR InterPro; IPR000630; Ribosomal_uS8.
DR InterPro; IPR047863; Ribosomal_uS8_CS.
DR InterPro; IPR035987; Ribosomal_uS8_sf.
DR PANTHER; PTHR11758:SF4; 37S RIBOSOMAL PROTEIN S8, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11758; 40S RIBOSOMAL PROTEIN S15A; 1.
DR Pfam; PF00410; Ribosomal_S8; 1.
DR SUPFAM; SSF56047; Ribosomal protein S8; 1.
DR PROSITE; PS00053; RIBOSOMAL_S8; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01302};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01302};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01302};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_01302}.
SQ SEQUENCE 131 AA; 14133 MW; 3116D4F517166A3B CRC64;
MSMSDPIADM LTRIRNAQTV SKTTVNMPSS KVKVAIANVL KDEGYIEDFA VTTEGGKAEL
KIGLKYYTGR PVIERIERVS RPGLRVYKGK NEIPSVMNGL GVAIVSTPQG VMTDRKARAT
GVGGEVLCYV A
//