ID   RS7_CAMJD               Reviewed;         156 AA.
AC   A7H4P6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=30S ribosomal protein S7 {ECO:0000255|HAMAP-Rule:MF_00480};
GN   Name=rpsG {ECO:0000255|HAMAP-Rule:MF_00480};
GN   OrderedLocusNames=JJD26997_1443;
OS   Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 /
OS   269.97).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1458 / RM4099 / 269.97;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT   "Complete genome sequence of Campylobacter jejuni subsp doylei 269.97
RT   isolated from human blood.";
RL   Submitted (JUL-2007) 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; CP000768; ABS43705.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7H4P6; -.
DR   SMR; A7H4P6; -.
DR   EnsemblBacteria; ABS43705; ABS43705; JJD26997_1443.
DR   KEGG; cjd:JJD26997_1443; -.
DR   HOGENOM; CLU_072226_1_1_7; -.
DR   OMA; NVMPHVE; -.
DR   Proteomes; UP000002302; 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_1000014169"
SQ   SEQUENCE   156 AA;  17692 MW;  C209D2FE0F75A1A0 CRC64;
     MRRRKAPVRE VLPDPIYGNK VITKFINSLM YDGKKSTATT IMYGALEAID KKGGEKKGID
     IFNDAIENIK PLLEVKSRRV GGATYQVPVE VRPARQQALA IRWIISFARK RSERTMIDKL
     AAELLDAANS KGASFKKKED TYKMAEANKA FAHYRW