(data stored in ACNUC7421 zone)

HOGENOM: BRAP9_1_PE1013

ID   BRAP9_1_PE1013                       STANDARD;      PRT;   100 AA.
AC   BRAP9_1_PE1013; D8ICZ9;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=30S ribosomal protein S12; (BRAP9_1.PE1013).
GN   Name=rpsL; OrderedLocusNames=BP951000_1031;
OS   BRACHYSPIRA PILOSICOLI 95/1000.
OC   Bacteria; Spirochaetes; Spirochaetales; Brachyspiraceae; Brachyspira.
OX   NCBI_TaxID=759914;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BRAP9_1.PE1013.
CC       Brachyspira pilosicoli 95/1000 chromosome, complete genome.
CC       1..5047 annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:D8ICZ9_BRAP9
CC   -!- FUNCTION: Interacts with and stabilizes bases of the 16S rRNA that
CC       are involved in tRNA selection in the A site and with the mRNA
CC       backbone. Located at the interface of the 30S and 50S subunits, it
CC       traverses the body of the 30S subunit contacting proteins on the
CC       other side and probably holding the rRNA structure together. The
CC       combined cluster of proteins S8, S12 and S17 appears to hold
CC       together the shoulder and platform of the 30S subunit (By
CC       similarity).
CC   -!- FUNCTION: With S4 and S5 plays an important role in translational
CC       accuracy (By similarity).
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S8
CC       and S17. May interact with IF1 in the 30S initiation complex (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the ribosomal protein S12P family.
CC   -!- GENE_FAMILY: HOG000040063 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D8ICZ9; -.
DR   EMBL; CP002025; ADK31022.1; -; Genomic_DNA.
DR   RefSeq; YP_003785523.1; NC_014330.1.
DR   GeneID; 9451150; -.
DR   GenomeReviews; CP002025_GR; BP951000_1031.
DR   KEGG; bpo:BP951000_1031; -.
DR   GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR016027; NA-bd_OB-fold-like.
DR   InterPro; IPR006032; Ribosomal_S12/S23.
DR   InterPro; IPR005679; Ribosomal_S12_bac.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   PANTHER; PTHR11652; Ribosomal_S12_23; 1.
DR   Pfam; PF00164; Ribosomal_S12; 1.
DR   PIRSF; PIRSF002133; Ribosomal_S12/S23; 1.
DR   PRINTS; PR01034; RIBOSOMALS12.
DR   SUPFAM; SSF50249; Nucleic_acid_OB; 1.
DR   TIGRFAMs; TIGR00981; RpsL_bact; 1.
DR   PROSITE; PS00055; RIBOSOMAL_S12; 1.
DR   HOGENOMDNA; BRAP9_1.PE1013; -.
KW   30S ribosomal protein S12;
KW   Complete proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding; tRNA-binding.
SQ   SEQUENCE   100 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKCPQREGVC TRVTTTTPKK PNSAMRKIAR VRITNGMEVT AYIPGIDHTL QEHNRVLIRG
     GRVKDLPGCR YHIVRGSREA SGVEKRMKSR SKYGTKKPKA
//

If you have problems or comments...

PBIL Back to PBIL home page