ID RS5_GRABC Reviewed; 190 AA.
AC Q0BUN3;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 01-MAY-2013, entry version 48.
DE RecName: Full=30S ribosomal protein S5;
GN Name=rpsE; OrderedLocusNames=GbCGDNIH1_0571;
OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Granulibacter.
OX NCBI_TaxID=391165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1260 / CGDNIH1;
RX PubMed=17827295; DOI=10.1128/JB.00793-07;
RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K.,
RA Sturdevant D.E., Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W.,
RA Holland S.M.;
RT "Genome sequence analysis of the emerging human pathogenic acetic acid
RT bacterium Granulibacter bethesdensis.";
RL J. Bacteriol. 189:8727-8736(2007).
CC -!- FUNCTION: With S4 and S12 plays an important role in translational
CC accuracy (By similarity).
CC -!- FUNCTION: Located at the back of the 30S subunit body where it
CC stabilizes the conformation of the head with respect to the body
CC (By similarity).
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S4
CC and S8 (By similarity).
CC -!- DOMAIN: The N-terminal domain interacts with the head of the 30S
CC subunit; the C-terminal domain interacts with the body and
CC contacts protein S4. The interaction surface between S4 and S5 is
CC involved in control of translational fidelity.
CC -!- SIMILARITY: Belongs to the ribosomal protein S5P family.
CC -!- SIMILARITY: Contains 1 S5 DRBM domain.
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DR EMBL; CP000394; ABI61469.1; -; Genomic_DNA.
DR RefSeq; YP_744392.1; NC_008343.1.
DR ProteinModelPortal; Q0BUN3; -.
DR SMR; Q0BUN3; 21-155.
DR STRING; 391165.GbCGDNIH1_0571; -.
DR EnsemblBacteria; ABI61469; ABI61469; GbCGDNIH1_0571.
DR GeneID; 4274908; -.
DR KEGG; gbe:GbCGDNIH1_0571; -.
DR PATRIC; 22077215; VBIGraBet83793_0599.
DR eggNOG; COG0098; -.
DR HOGENOM; HOG000072595; -.
DR KO; K02988; -.
DR OMA; HNVVKAT; -.
DR ProtClustDB; PRK00550; -.
DR BioCyc; GBET391165:GHON-632-MONOMER; -.
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:HAMAP.
DR GO; GO:0006412; P:translation; IEA:HAMAP.
DR Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR HAMAP; MF_01307_B; Ribosomal_S5_B; 1; -.
DR InterPro; IPR014720; dsRNA-bd-like_dom.
DR InterPro; IPR000851; Ribosomal_S5.
DR InterPro; IPR005712; Ribosomal_S5_bac-type.
DR InterPro; IPR005324; Ribosomal_S5_C.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR013810; Ribosomal_S5_N.
DR InterPro; IPR018192; Ribosomal_S5_N_CS.
DR PANTHER; PTHR13718; PTHR13718; 1.
DR Pfam; PF00333; Ribosomal_S5; 1.
DR Pfam; PF03719; Ribosomal_S5_C; 1.
DR SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1.
DR TIGRFAMs; TIGR01021; rpsE_bact; 1.
DR PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR PROSITE; PS50881; S5_DSRBD; 1.
PE 3: Inferred from homology;
KW Complete proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1 190 30S ribosomal protein S5.
FT /FTId=PRO_0000323131.
FT DOMAIN 19 82 S5 DRBM.
SQ SEQUENCE 190 AA; 20347 MW; 868E34235BF815D2 CRC64;
MAREPREGRG GREREADDII DKLVTINRVA KVVKGGRRFA FAALVVVGDQ KGRVGYGAGK
AREVPEAIRK ATERAKRSMI RVPMKEGRTL HHDVYGHFGA GKVVLRSATA GTGIIAGGPM
RAVFESLGIG DVVAKSLGSR NPHNMVKATF AALERCSSPR SVASRRGKKV SDILGRREPV
AGQEGEEAHA
//
