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Database: UniProt
Entry: A0A248THG5_9BACI
LinkDB: A0A248THG5_9BACI
Original site: A0A248THG5_9BACI 
ID   A0A248THG5_9BACI        Unreviewed;       156 AA.
AC   A0A248THG5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Small ribosomal subunit protein uS7 {ECO:0000256|HAMAP-Rule:MF_00480};
GN   Name=rpsG {ECO:0000256|HAMAP-Rule:MF_00480};
GN   ORFNames=CKF48_10155 {ECO:0000313|EMBL:ASV67657.1};
OS   Cytobacillus kochii.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Cytobacillus.
OX   NCBI_TaxID=859143 {ECO:0000313|EMBL:ASV67657.1, ECO:0000313|Proteomes:UP000215137};
RN   [1] {ECO:0000313|EMBL:ASV67657.1, ECO:0000313|Proteomes:UP000215137}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BDGP4 {ECO:0000313|EMBL:ASV67657.1,
RC   ECO:0000313|Proteomes:UP000215137};
RA   Wan K.H., Yu C., Park S., Hammonds A.S., Booth B.W., Celniker S.E.;
RT   "Complete Genome Sequence of Bacillus kochii Oregon-R-modENCODE STRAIN
RT   BDGP4, isolated from Drosophila melanogaster gut.";
RL   Submitted (AUG-2017) 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:0000256|HAMAP-
CC       Rule:MF_00480}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S9 and
CC       S11. {ECO:0000256|HAMAP-Rule:MF_00480}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS7 family.
CC       {ECO:0000256|ARBA:ARBA00007151, ECO:0000256|HAMAP-Rule:MF_00480,
CC       ECO:0000256|RuleBase:RU003619}.
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DR   EMBL; CP022983; ASV67657.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A248THG5; -.
DR   KEGG; bko:CKF48_10155; -.
DR   OrthoDB; 9807653at2; -.
DR   Proteomes; UP000215137; 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   CDD; cd14869; uS7_Bacteria; 1.
DR   Gene3D; 1.10.455.10; Ribosomal protein S7 domain; 1.
DR   HAMAP; MF_00480_B; Ribosomal_S7_B; 1.
DR   InterPro; IPR000235; Ribosomal_uS7.
DR   InterPro; IPR005717; Ribosomal_uS7_bac/org-type.
DR   InterPro; IPR020606; Ribosomal_uS7_CS.
DR   InterPro; IPR023798; Ribosomal_uS7_dom.
DR   InterPro; IPR036823; Ribosomal_uS7_dom_sf.
DR   NCBIfam; TIGR01029; rpsG_bact; 1.
DR   PANTHER; PTHR11205:SF19; 28S RIBOSOMAL PROTEIN S7, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11205; RIBOSOMAL PROTEIN S7; 1.
DR   Pfam; PF00177; Ribosomal_S7; 1.
DR   PIRSF; PIRSF002122; RPS7p_RPS7a_RPS5e_RPS7o; 1.
DR   SUPFAM; SSF47973; Ribosomal protein S7; 1.
DR   PROSITE; PS00052; RIBOSOMAL_S7; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000215137};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_00480};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_00480};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00480};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_00480}; tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00480}.
FT   DOMAIN          1..149
FT                   /note="Small ribosomal subunit protein uS7"
FT                   /evidence="ECO:0000259|Pfam:PF00177"
SQ   SEQUENCE   156 AA;  17866 MW;  E1B5ABE5E35289CB CRC64;
     MPRKGPVAKR DVLPDPIYNS KLVSRLINKM MVDGKRGKSQ AILYNAFDII SERTGKEPME
     VFDQALKNIM PVLEVRARRV GGANYQVPVE VRPDRRTTLG LRWLVNYARL RGEKTMEERL
     ANEILDAANN TGASVKKRED THKMAEANKA FAHYRW
//
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