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Database: UniProt/TrEMBL
Entry: G2IW69_PSEUL
LinkDB: G2IW69_PSEUL
Original site: G2IW69_PSEUL 
ID   G2IW69_PSEUL            Unreviewed;       206 AA.
AC   G2IW69;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   22-JUL-2015, entry version 23.
DE   RecName: Full=30S ribosomal protein S4 {ECO:0000256|HAMAP-Rule:MF_01306};
GN   Name=rpsD {ECO:0000256|HAMAP-Rule:MF_01306};
GN   OrderedLocusNames=NH8B_0383 {ECO:0000313|EMBL:BAK75224.1};
OS   Pseudogulbenkiania sp. (strain NH8B).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Pseudogulbenkiania.
OX   NCBI_TaxID=748280 {ECO:0000313|Proteomes:UP000001274};
RN   [1] {ECO:0000313|Proteomes:UP000001274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NH8B {ECO:0000313|Proteomes:UP000001274};
RX   PubMed=22038961; DOI=10.1128/JB.06127-11;
RA   Ishii S., Tago T., Nishizawa T., Oshima K., Hattori M., Senoo K.;
RT   "Complete genome sequence of the denitrifying and N(2)O-reducing
RT   bacterium Pseudogulbenkiania sp. strain NH8B.";
RL   J. Bacteriol. 193:6395-6396(2011).
CC   -!- FUNCTION: One of the primary rRNA binding proteins, it binds
CC       directly to 16S rRNA where it nucleates assembly of the body of
CC       the 30S subunit. {ECO:0000256|HAMAP-Rule:MF_01306}.
CC   -!- FUNCTION: With S5 and S12 plays an important role in translational
CC       accuracy. {ECO:0000256|HAMAP-Rule:MF_01306}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S5.
CC       The interaction surface between S4 and S5 is involved in control
CC       of translational fidelity. {ECO:0000256|HAMAP-Rule:MF_01306}.
CC   -!- SIMILARITY: Belongs to the ribosomal protein S4P family.
CC       {ECO:0000256|HAMAP-Rule:MF_01306, ECO:0000256|RuleBase:RU003699}.
CC   -!- SIMILARITY: Contains 1 S4 RNA-binding domain. {ECO:0000256|HAMAP-
CC       Rule:MF_01306, ECO:0000256|RuleBase:RU003699}.
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DR   EMBL; AP012224; BAK75224.1; -; Genomic_DNA.
DR   RefSeq; WP_008955660.1; NC_016002.1.
DR   EnsemblBacteria; BAK75224; BAK75224; NH8B_0383.
DR   KEGG; pse:NH8B_0383; -.
DR   KO; K02986; -.
DR   BioCyc; PSP748280:GHJ9-383-MONOMER; -.
DR   Proteomes; UP000001274; Chromosome.
DR   GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 1.10.1050.10; -; 1.
DR   Gene3D; 3.10.290.10; -; 1.
DR   HAMAP; MF_01306_B; Ribosomal_S4_B; 1.
DR   InterPro; IPR022801; Ribosomal_S4/S9.
DR   InterPro; IPR001912; Ribosomal_S4/S9_N.
DR   InterPro; IPR005709; Ribosomal_S4_bac-type.
DR   InterPro; IPR018079; Ribosomal_S4_CS.
DR   InterPro; IPR002942; S4_RNA-bd.
DR   PANTHER; PTHR11831; PTHR11831; 1.
DR   Pfam; PF00163; Ribosomal_S4; 1.
DR   Pfam; PF01479; S4; 1.
DR   SMART; SM00363; S4; 1.
DR   TIGRFAMs; TIGR01017; rpsD_bact; 1.
DR   PROSITE; PS00632; RIBOSOMAL_S4; 1.
DR   PROSITE; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001274};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001274};
KW   Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_01306,
KW   ECO:0000256|RuleBase:RU003699};
KW   Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_01306,
KW   ECO:0000256|RuleBase:RU003699};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01306};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01306}.
FT   DOMAIN       96    159       S4 RNA-binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_01306}.
SQ   SEQUENCE   206 AA;  23099 MW;  6A6EE42E38BBD8BE CRC64;
     MARYIGPKCK LARREGTDLF LKSARRALDS KCKLDSIPGQ HGARKSRLSD YGVQLREKQK
     IRRIYGVLER QFRNYFAEAS RLKGSTGENL LKLLESRLDN VVYRMGFGST RAEARQLVSH
     KAIVVNGQVV NIPSFQVKAG DVVAIREKAK KQARIVEGLA LAEQGGFPSW VSVDPKKMEG
     VFKSAPERSE LAGDINEQLV VEFYSK
//
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