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Database: UniProt
Entry: A5IHP2
LinkDB: A5IHP2
Original site: A5IHP2 
ID   RS4_LEGPC               Reviewed;         206 AA.
AC   A5IHP2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   14-MAY-2014, entry version 45.
DE   RecName: Full=30S ribosomal protein S4;
GN   Name=rpsD; OrderedLocusNames=LPC_2991;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S.,
RA   Schunder E., Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a
RT   mobile genomic island.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC   -!- FUNCTION: With S5 and S12 plays an important role in translational
CC       accuracy (By similarity).
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 (By similarity).
CC   -!- SIMILARITY: Belongs to the ribosomal protein S4P family.
CC   -!- SIMILARITY: Contains 1 S4 RNA-binding domain.
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DR   EMBL; CP000675; ABQ56892.1; -; Genomic_DNA.
DR   RefSeq; YP_001252238.1; NC_009494.2.
DR   ProteinModelPortal; A5IHP2; -.
DR   SMR; A5IHP2; 2-206.
DR   STRING; 400673.LPC_2991; -.
DR   EnsemblBacteria; ABQ56892; ABQ56892; LPC_2991.
DR   GeneID; 5182769; -.
DR   KEGG; lpc:LPC_2991; -.
DR   PATRIC; 22312593; VBILegPne45588_3100.
DR   eggNOG; COG0522; -.
DR   HOGENOM; HOG000221003; -.
DR   KO; K02986; -.
DR   OMA; TCKLSRR; -.
DR   OrthoDB; EOG6N3CXM; -.
DR   BioCyc; LPNE400673:GCIT-421-MONOMER; -.
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; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN         1    206       30S ribosomal protein S4.
FT                                /FTId=PRO_0000322310.
FT   DOMAIN       96    161       S4 RNA-binding.
SQ   SEQUENCE   206 AA;  23261 MW;  105B2EA449FC0663 CRC64;
     MARYLGPKCK LSRREGCDLL LKSGVRDHKS KCKSEKLPGQ HGDKKPRLNS YGIQLREKQK
     IRRLYGILEK QFRNYYKKAA RQKGSTGENL MALLERRLDN VVYRMGFAST RAEARQLVAH
     KAILVNDKVV NVPSFLVNPG DTVSVRQKAK NQGRIQAALA LSEQRAPCDW ITVDTGSFKG
     TFSTAPTLMD LSSDYNVNLV VELYSK
//
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