RS7_GEOSE
ID RS7_GEOSE Reviewed; 156 AA.
AC P22744;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=30S ribosomal protein S7;
DE Short=BS7;
GN Name=rpsG;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-10; 12-21;
RP 30-41; 57-73; 80-92; 110-127 AND 139-155.
RC STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924;
RX PubMed=1368664; DOI=10.1271/bbb1961.55.207;
RA Kimura M.;
RT "The nucleotide sequences of Bacillus stearothermophilus ribosomal protein
RT S12 and S7 genes: comparison with the str operon of Escherichia coli.";
RL Agric. Biol. Chem. 55:207-213(1991).
RN [2]
RP PROTEIN SEQUENCE OF 2-21 AND 108-127, AND CROSS-LINKING TO RRNA.
RC STRAIN=799;
RX PubMed=7556101; DOI=10.1002/j.1460-2075.1995.tb00137.x;
RA Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.;
RT "Protein-rRNA binding features and their structural and functional
RT implications in ribosomes as determined by cross-linking studies.";
RL EMBO J. 14:4578-4588(1995).
RN [3]
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 [4]
RP MUTAGENESIS.
RX PubMed=10561602; DOI=10.1046/j.1432-1327.1999.00901.x;
RA Miyamoto A., Usui M., Yamasaki N., Yamada N., Kuwano E., Tanaka I.,
RA Kimura M.;
RT "Role of the N-terminal region of ribosomal protein S7 in its interaction
RT with 16S rRNA which binds to the concavity formed by the beta-ribbon arm
RT and the alpha-helix.";
RL Eur. J. Biochem. 266:591-598(1999).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND SEQUENCE REVISION TO 60 AND 112.
RX PubMed=9331423; DOI=10.1016/s0969-2126(97)00270-0;
RA Hosaka H., Nakagawa A., Tanaka I., Harada N., Sano K., Kimura M., Yao M.,
RA Wakatsuki S.;
RT "Ribosomal protein S7: a new RNA-binding motif with structural similarities
RT to a DNA architectural factor.";
RL Structure 5:1199-1208(1997).
CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC to 16S rRNA where it nucleates assembly of the head domain of the 30S
CC subunit. Is located at the subunit interface close to the decoding
CC center, probably blocks exit of the E-site tRNA (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S9 and
CC S11 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS7 family.
CC {ECO:0000305}.
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DR PIR; JG0008; JG0008.
DR PDB; 1HUS; X-ray; 2.50 A; A=2-156.
DR PDBsum; 1HUS; -.
DR AlphaFoldDB; P22744; -.
DR SMR; P22744; -.
DR EvolutionaryTrace; P22744; -.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.455.10; -; 1.
DR HAMAP; MF_00480_B; Ribosomal_S7_B; 1.
DR InterPro; IPR000235; Ribosomal_S5/S7.
DR InterPro; IPR005717; Ribosomal_S7_bac/org-type.
DR InterPro; IPR020606; Ribosomal_S7_CS.
DR InterPro; IPR023798; Ribosomal_S7_dom.
DR InterPro; IPR036823; Ribosomal_S7_dom_sf.
DR PANTHER; PTHR11205; PTHR11205; 1.
DR Pfam; PF00177; Ribosomal_S7; 1.
DR PIRSF; PIRSF002122; RPS7p_RPS7a_RPS5e_RPS7o; 1.
DR SUPFAM; SSF47973; SSF47973; 1.
DR TIGRFAMs; TIGR01029; rpsG_bact; 1.
DR PROSITE; PS00052; RIBOSOMAL_S7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1368664,
FT ECO:0000269|PubMed:4607606, ECO:0000269|PubMed:7556101"
FT CHAIN 2..156
FT /note="30S ribosomal protein S7"
FT /id="PRO_0000124218"
FT MUTAGEN 2..11
FT /note="Missing: No binding to 16S RRNA."
FT /evidence="ECO:0000269|PubMed:10561602"
FT CONFLICT 60
FT /note="E -> K (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="N -> G (in Ref. 1; AA sequence and 2; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:1HUS"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:1HUS"
FT HELIX 36..54
FT /evidence="ECO:0007829|PDB:1HUS"
FT HELIX 58..69
FT /evidence="ECO:0007829|PDB:1HUS"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:1HUS"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:1HUS"
FT HELIX 93..110
FT /evidence="ECO:0007829|PDB:1HUS"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1HUS"
FT HELIX 116..128
FT /evidence="ECO:0007829|PDB:1HUS"
FT HELIX 133..147
FT /evidence="ECO:0007829|PDB:1HUS"
SQ SEQUENCE 156 AA; 18046 MW; 818A409F89C6A197 CRC64;
MPRRGPVAKR DVLPDPIYNS KLVTRLINKI MIDGKKSKAQ KILYTAFDII RERTGKDPME
VFEQALKNVM PVLEVRARRV GGANYQVPVE VRPDRRVSLG LRWLVQYARL RNEKTMEERL
ANEIMDAANN TGAAVKKRED THKMAEANKA FAHYRW
