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Database: UniProt
Entry: Q0I088
LinkDB: Q0I088
Original site: Q0I088 
ID   RS5_SHESR               Reviewed;         167 AA.
AC   Q0I088;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   01-MAY-2013, entry version 50.
DE   RecName: Full=30S ribosomal protein S5;
GN   Name=rpsE; OrderedLocusNames=Shewmr7_0211;
OS   Shewanella sp. (strain MR-7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60481;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-7;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nealson K., Konstantinidis K., Klappenbach J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. MR-7.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000444; ABI41217.1; -; Genomic_DNA.
DR   RefSeq; YP_736274.1; NC_008322.1.
DR   ProteinModelPortal; Q0I088; -.
DR   SMR; Q0I088; 11-159.
DR   STRING; 60481.Shewmr7_0211; -.
DR   EnsemblBacteria; ABI41217; ABI41217; Shewmr7_0211.
DR   GeneID; 4255673; -.
DR   KEGG; shm:Shewmr7_0211; -.
DR   PATRIC; 23585266; VBISheSp85603_0224.
DR   eggNOG; COG0098; -.
DR   HOGENOM; HOG000072595; -.
DR   KO; K02988; -.
DR   OMA; HNVVKAT; -.
DR   ProtClustDB; PRK00550; -.
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    167       30S ribosomal protein S5.
FT                                /FTId=PRO_0000323201.
FT   DOMAIN       12     75       S5 DRBM.
SQ   SEQUENCE   167 AA;  17741 MW;  E554F947D06CBBB8 CRC64;
     MAKLEAQQKD DLQEKLIAVN RVSKVVKGGR IFSFTALTVV GDGNGKVGYG YGKAREVPAA
     IQKAMEKARR NMVTVELNAG TLHHPVKGRH TGSRVYMQPA SQGTGIIAGG AMRAVLEVAG
     VHNVLSKAYG STNPINIVRA TVDALVHMKS PSQIAAKRGL NVDEIRG
//
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