ID   RS7_LEPBP               Reviewed;         157 AA.
AC   B0SSI1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=30S ribosomal protein S7 {ECO:0000255|HAMAP-Rule:MF_00480};
GN   Name=rpsG {ECO:0000255|HAMAP-Rule:MF_00480}; OrderedLocusNames=LEPBI_I1968;
OS   Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=456481;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Patoc 1 / ATCC 23582 / Paris;
RX   PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA   Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA   Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA   Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA   Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT   "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT   into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL   PLoS ONE 3:E1607-E1607(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; CP000786; ABZ98071.1; -; Genomic_DNA.
DR   RefSeq; WP_012388943.1; NC_010602.1.
DR   AlphaFoldDB; B0SSI1; -.
DR   SMR; B0SSI1; -.
DR   STRING; 456481.LEPBI_I1968; -.
DR   KEGG; lbi:LEPBI_I1968; -.
DR   HOGENOM; CLU_072226_1_1_12; -.
DR   OMA; NVMPHVE; -.
DR   OrthoDB; 1540940at2; -.
DR   BioCyc; LBIF456481:LEPBI_RS09725-MON; -.
DR   Proteomes; UP000001847; Chromosome I.
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..157
FT                   /note="30S ribosomal protein S7"
FT                   /id="PRO_1000125963"
SQ   SEQUENCE   157 AA;  18017 MW;  5DF0974AFB5F9F5F CRC64;
     MSRRRGKVEP RHIEGDPKYN DKVISKFINC LMVDGKKSVA ESVFYDALEV IAKKTGQDPF
     AVFQEALENA KPQVEVKSRR VGGVTYQVPI EVRPERRLAL GIRWLIKYSR GRNEKSMKNK
     LAAEFMEAQK GTGSAIKKKE DIRKMADANK AFSHYRW