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 01-MAY-2013, entry version 40.
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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; THGHILV; -.
DR ProtClustDB; PRK05327; -.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:HAMAP.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA: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
//