RS8_GEOSE
ID RS8_GEOSE Reviewed; 131 AA.
AC P56209;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=30S ribosomal protein S8 {ECO:0000255|HAMAP-Rule:MF_01302};
DE Short=BS8;
GN Name=rpsH {ECO:0000255|HAMAP-Rule:MF_01302};
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP PROTEIN SEQUENCE OF 2-131.
RX PubMed=1764513; DOI=10.1016/0300-9084(91)90045-3;
RA Arndt E., Scholzen T., Kromer W., Hatakeyama T., Kimura M.;
RT "Primary structures of ribosomal proteins from the archaebacterium
RT Halobacterium marismortui and the eubacterium Bacillus
RT stearothermophilus.";
RL Biochimie 73:657-668(1991).
RN [2]
RP PROTEIN SEQUENCE OF 2-16.
RC STRAIN=DSM 13240 / CIP 106956 / 10;
RX PubMed=4607606; DOI=10.1016/0014-5793(74)80391-1;
RA Yaguchi M., Matheson A.T., Visentin L.P.;
RT "Procaryotic ribosomal proteins: N-terminal sequence homologies and
RT structural correspondence of 30 S ribosomal proteins from Escherichia coli
RT and Bacillus stearothermophilus.";
RL FEBS Lett. 46:296-300(1974).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=8805594; DOI=10.1016/s0969-2126(96)00115-3;
RA Davies C., Ramakrishnan V., White S.W.;
RT "Structural evidence for specific S8-RNA and S8-protein interactions within
RT the 30S ribosomal subunit: ribosomal protein S8 from Bacillus
RT stearothermophilus at 1.9-A resolution.";
RL Structure 4:1093-1104(1996).
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 PDB; 1SEI; X-ray; 1.90 A; A/B=2-131.
DR PDBsum; 1SEI; -.
DR AlphaFoldDB; P56209; -.
DR SMR; P56209; -.
DR EvolutionaryTrace; P56209; -.
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 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; Direct protein sequencing; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1764513,
FT ECO:0000269|PubMed:4607606"
FT CHAIN 2..131
FT /note="30S ribosomal protein S8"
FT /id="PRO_0000126366"
FT CONFLICT 13
FT /note="A -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 5..19
FT /evidence="ECO:0007829|PDB:1SEI"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:1SEI"
FT HELIX 31..42
FT /evidence="ECO:0007829|PDB:1SEI"
FT STRAND 45..56
FT /evidence="ECO:0007829|PDB:1SEI"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:1SEI"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:1SEI"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1SEI"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:1SEI"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:1SEI"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:1SEI"
FT HELIX 114..120
FT /evidence="ECO:0007829|PDB:1SEI"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:1SEI"
SQ SEQUENCE 131 AA; 14760 MW; 64F5C838CF286E3E CRC64;
MVMTDPIADM LTAIRNANMV RHEKLEVPAS KIKREIAEIL KREGFIRDYE YIEDNKQGIL
RIFLKYGPNE RVITGLKRIS KPGLRVYVKA HEVPRVLNGL GIAILSTSQG VLTDKEARQK
GTGGEIIAYV I