RS7_ACIC1
ID RS7_ACIC1 Reviewed; 156 AA.
AC A0LRL6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=30S ribosomal protein S7 {ECO:0000255|HAMAP-Rule:MF_00480};
GN Name=rpsG {ECO:0000255|HAMAP-Rule:MF_00480}; OrderedLocusNames=Acel_0302;
OS Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC Bacteria; Actinobacteria; Acidothermales; Acidothermaceae; Acidothermus.
OX NCBI_TaxID=351607;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43068 / DSM 8971 / 11B;
RX PubMed=19270083; DOI=10.1101/gr.084848.108;
RA Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT "Complete genome of the cellulolytic thermophile Acidothermus
RT cellulolyticus 11B provides insights into its ecophysiological and
RT evolutionary adaptations.";
RL Genome Res. 19:1033-1043(2009).
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; CP000481; ABK52076.1; -; Genomic_DNA.
DR RefSeq; WP_011719139.1; NC_008578.1.
DR AlphaFoldDB; A0LRL6; -.
DR SMR; A0LRL6; -.
DR STRING; 351607.Acel_0302; -.
DR EnsemblBacteria; ABK52076; ABK52076; Acel_0302.
DR KEGG; ace:Acel_0302; -.
DR eggNOG; COG0049; Bacteria.
DR HOGENOM; CLU_072226_1_1_11; -.
DR OMA; NVMPHVE; -.
DR OrthoDB; 1540940at2; -.
DR Proteomes; UP000008221; 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_1000014134"
SQ SEQUENCE 156 AA; 17711 MW; C8277ACCECEA5A83 CRC64;
MPRKGPAPKR PIVSDPVYGS PLVTALINKV LQRGKRSLAE RIVYNALEGC RARTGTDPLI
TLKRALDNVR PTLEVRSRRV GGATYQVPVE VRPQRSTSLA LRWIVHYAKL RREKTMIERL
TNELLDASNG LGASVKRRED THKMAESNRA FAHYRW