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Database: UniProt
Entry: Q17ZC2
LinkDB: Q17ZC2
Original site: Q17ZC2 
ID   RS5_HELAH               Reviewed;         153 AA.
AC   Q17ZC2;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-SEP-2014, entry version 59.
DE   RecName: Full=30S ribosomal protein S5;
GN   Name=rpsE; OrderedLocusNames=Hac_0152;
OS   Helicobacter acinonychis (strain Sheeba).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=382638;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sheeba;
RX   PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA   Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H.,
RA   Morelli G., Gressmann H., Achtman M., Schuster S.C.;
RT   "Who ate whom? Adaptive Helicobacter genomic changes that accompanied
RT   a host jump from early humans to large felines.";
RL   PLoS Genet. 2:1097-1110(2006).
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; AM260522; CAJ99004.1; -; Genomic_DNA.
DR   RefSeq; WP_011577122.1; NC_008229.1.
DR   RefSeq; YP_664003.1; NC_008229.1.
DR   ProteinModelPortal; Q17ZC2; -.
DR   SMR; Q17ZC2; 11-152.
DR   STRING; 382638.Hac_0152; -.
DR   EnsemblBacteria; CAJ99004; CAJ99004; Hac_0152.
DR   GeneID; 4177145; -.
DR   KEGG; hac:Hac_0152; -.
DR   PATRIC; 20584228; VBIHelAci71660_0147.
DR   eggNOG; COG0098; -.
DR   HOGENOM; HOG000072595; -.
DR   KO; K02988; -.
DR   OMA; PYNVVHA; -.
DR   OrthoDB; EOG6FJNM5; -.
DR   BioCyc; HACI382638:GJAU-139-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:UniProtKB-HAMAP.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-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_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; SSF54211; 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    153       30S ribosomal protein S5.
FT                                /FTId=PRO_0000323134.
FT   DOMAIN       15     78       S5 DRBM.
SQ   SEQUENCE   153 AA;  16505 MW;  F4DCC79868953B47 CRC64;
     MTERKGMEEI NREEFQEVVV NVGRVTKVVK GGRRFRFNAL VVVGNKNGLV GFGLGKAKEV
     PDAIKKAVDD AFKNLIHVTI KGTTIAHDIE HKYNASRILL KPASEGTGVI AGGSTRPIVE
     LAGIKDILTK SLGSNNPYNV VHATFDALAK IKA
//
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