ID   RS7_CLOBB               Reviewed;         156 AA.
AC   B2TIH1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=30S ribosomal protein S7 {ECO:0000255|HAMAP-Rule:MF_00480};
GN   Name=rpsG {ECO:0000255|HAMAP-Rule:MF_00480}; OrderedLocusNames=CLL_A0234;
OS   Clostridium botulinum (strain Eklund 17B / Type B).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=935198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eklund 17B / Type B;
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete sequence of Clostridium botulinum strain Eklund.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00480}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S9 and
CC       S11. {ECO:0000255|HAMAP-Rule:MF_00480}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS7 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00480}.
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DR   EMBL; CP001056; ACD24776.1; -; Genomic_DNA.
DR   RefSeq; WP_003372509.1; NC_018648.1.
DR   AlphaFoldDB; B2TIH1; -.
DR   SMR; B2TIH1; -.
DR   EnsemblBacteria; ACD24776; ACD24776; CLL_A0234.
DR   KEGG; cbk:CLL_A0234; -.
DR   PATRIC; fig|935198.13.peg.208; -.
DR   HOGENOM; CLU_072226_1_1_9; -.
DR   OMA; NVMPHVE; -.
DR   OrthoDB; 1540940at2; -.
DR   Proteomes; UP000001195; Chromosome.
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   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW   tRNA-binding.
FT   CHAIN           1..156
FT                   /note="30S ribosomal protein S7"
FT                   /id="PRO_1000125919"
SQ   SEQUENCE   156 AA;  17726 MW;  AF920DE85AB940FF CRC64;
     MPRKGHIAKR DVLPDPVYNS KVVTKFINSI MEDGKKGVAQ KICYEAFELI AQRSGKEALE
     VFEEAMNNVM PLLEVKARRI GGATYQVPME VRTERRQTLG IRWMLIAARK RGEKLMCERV
     AGELLDASNN TGAAVKKRED THKMAEANKA FAHYRY