ID   RS7_PELTS               Reviewed;         156 AA.
AC   A5D5I6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=30S ribosomal protein S7 {ECO:0000255|HAMAP-Rule:MF_00480};
GN   Name=rpsG {ECO:0000255|HAMAP-Rule:MF_00480}; OrderedLocusNames=PTH_0316;
OS   Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC   Pelotomaculum.
OX   NCBI_TaxID=370438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13744 / JCM 10971 / SI;
RX   PubMed=18218977; DOI=10.1101/gr.7136508;
RA   Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT   "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT   evolution in anaerobic microbiota.";
RL   Genome Res. 18:442-448(2008).
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; AP009389; BAF58497.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5D5I6; -.
DR   SMR; A5D5I6; -.
DR   STRING; 370438.PTH_0316; -.
DR   EnsemblBacteria; BAF58497; BAF58497; PTH_0316.
DR   KEGG; pth:PTH_0316; -.
DR   eggNOG; COG0049; Bacteria.
DR   HOGENOM; CLU_072226_1_1_9; -.
DR   OMA; NVMPHVE; -.
DR   Proteomes; UP000006556; 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   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding; tRNA-binding.
FT   CHAIN           1..156
FT                   /note="30S ribosomal protein S7"
FT                   /id="PRO_1000081291"
SQ   SEQUENCE   156 AA;  17591 MW;  4BCA35B81661F663 CRC64;
     MPRRGAVPKR EVLPDPVYQS KVLTKLINQV MLKGKKSLAE SIVYGAMDII KEKTGKNPLE
     VFETAMKNVM PVLEVKARRV GGANYQVPVE VRHDRRQTLA IRWLTNYARE RAGKSMKEKL
     ANEIMDAAAG TGGAVKKKED THKMAEANKA FAHYRW