ID   RS7_CLOBK               Reviewed;         156 AA.
AC   B1IGF8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=30S ribosomal protein S7 {ECO:0000255|HAMAP-Rule:MF_00480};
GN   Name=rpsG {ECO:0000255|HAMAP-Rule:MF_00480}; OrderedLocusNames=CLD_1020;
OS   Clostridium botulinum (strain Okra / Type B1).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okra / Type B1;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
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; CP000939; ACA44445.1; -; Genomic_DNA.
DR   RefSeq; WP_003402983.1; NC_010516.1.
DR   AlphaFoldDB; B1IGF8; -.
DR   SMR; B1IGF8; -.
DR   PRIDE; B1IGF8; -.
DR   EnsemblBacteria; ACA44445; ACA44445; CLD_1020.
DR   KEGG; cbb:CLD_1020; -.
DR   HOGENOM; CLU_072226_1_1_9; -.
DR   OMA; NVMPHVE; -.
DR   Proteomes; UP000008541; 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_1000125920"
SQ   SEQUENCE   156 AA;  17700 MW;  75DA1ECFE76B38A3 CRC64;
     MPRKGHIAKR DVLPDPLYNS KVVTKLINSI MLDGKRGVAQ KICYDAFEII GEKSGKDAME
     VFETAMNNIM PLLEVKARRI GGATYQVPIE VRPERRQTLG IRWMLIAARK RGERSMRERL
     AGELLDASNN TGAAVKKRED THKMAEANKA FAHYRY