RS8_AQUAE
ID RS8_AQUAE Reviewed; 168 AA.
AC O67566;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=30S ribosomal protein S8 {ECO:0000255|HAMAP-Rule:MF_01302};
GN Name=rpsH {ECO:0000255|HAMAP-Rule:MF_01302}; OrderedLocusNames=aq_1651;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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:0000255|HAMAP-Rule:MF_01302}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S5 and
CC S12. {ECO:0000255|HAMAP-Rule:MF_01302}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS8 family.
CC {ECO:0000255|HAMAP-Rule:MF_01302}.
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DR EMBL; AE000657; AAC07538.1; -; Genomic_DNA.
DR PIR; E70442; E70442.
DR RefSeq; NP_214132.1; NC_000918.1.
DR RefSeq; WP_010881069.1; NC_000918.1.
DR PDB; 3RF2; X-ray; 2.16 A; A=1-168.
DR PDBsum; 3RF2; -.
DR AlphaFoldDB; O67566; -.
DR SMR; O67566; -.
DR STRING; 224324.aq_1651; -.
DR EnsemblBacteria; AAC07538; AAC07538; aq_1651.
DR KEGG; aae:aq_1651; -.
DR PATRIC; fig|224324.8.peg.1272; -.
DR eggNOG; COG0096; Bacteria.
DR HOGENOM; CLU_098428_0_2_0; -.
DR InParanoid; O67566; -.
DR OMA; FDQGYIL; -.
DR OrthoDB; 1692188at2; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01302_B; Ribosomal_S8_B; 1.
DR InterPro; IPR000630; Ribosomal_S8.
DR InterPro; IPR035987; Ribosomal_S8_sf.
DR PANTHER; PTHR11758; PTHR11758; 1.
DR Pfam; PF00410; Ribosomal_S8; 1.
DR SUPFAM; SSF56047; SSF56047; 1.
DR PROSITE; PS00053; RIBOSOMAL_S8; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..168
FT /note="30S ribosomal protein S8"
FT /id="PRO_0000126354"
FT REGION 59..93
FT /note="Not found in other S8 sequences"
FT HELIX 6..19
FT /evidence="ECO:0007829|PDB:3RF2"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:3RF2"
FT HELIX 31..42
FT /evidence="ECO:0007829|PDB:3RF2"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:3RF2"
FT HELIX 54..69
FT /evidence="ECO:0007829|PDB:3RF2"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:3RF2"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:3RF2"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:3RF2"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:3RF2"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:3RF2"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:3RF2"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:3RF2"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:3RF2"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:3RF2"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:3RF2"
FT HELIX 151..156
FT /evidence="ECO:0007829|PDB:3RF2"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:3RF2"
SQ SEQUENCE 168 AA; 19458 MW; 4A404F2429B7D97C CRC64;
MSAVDPIADM FSAIKNAIMR RDDFLYVPSS KLKERILDVL KKEGFIQDWE ALKGEKYEEE
YKKMKELAEK SPNPKMKRYL KQLEEYNKGT QYPIKIYLKY LDPKKRKSAI TNIVKVSKGG
RRVYAGVRTM PYVKRGLGIA IVSTDAGVMT DHEARRMRKG GEVIAFVW