(data stored in SCRATCH zone)

HOGENOM: BOPER1_1_PE10

ID   BOPER1_1_PE10                        STANDARD;      PRT;   232 AA.
AC   BOPER1_1_PE10; Q7W0S2;
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=50S ribosomal protein L1; (BOPER1_1.PE10).
GN   Name=rplA; OrderedLocusNames=BP0011;
OS   BORDETELLA PERTUSSIS TOHAMA I.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257313;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BOPER1_1.PE10.
CC       Bordetella pertussis Tohama I, complete genome.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:RL1_BORPE
CC   -!- FUNCTION: Binds directly to 23S rRNA. The L1 stalk is quite mobile
CC       in the ribosome, and is involved in E site tRNA release (By
CC       similarity).
CC   -!- FUNCTION: Protein L1 is also a translational repressor protein, it
CC       controls the translation of the L11 operon by binding to its mRNA
CC       (By similarity).
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit.
CC   -!- SIMILARITY: Belongs to the ribosomal protein L1P family.
CC   -!- GENE_FAMILY: HOG000207015 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q7W0S2; -.
DR   EMBL; BX640411; CAE40391.1; -; Genomic_DNA.
DR   RefSeq; NP_878929.1; NC_002929.2.
DR   ProteinModelPortal; Q7W0S2; -.
DR   SMR; Q7W0S2; 6-227.
DR   GeneID; 2664704; -.
DR   GenomeReviews; BX470248_GR; BP0011.
DR   KEGG; bpe:BP0011; -.
DR   OMA; KAGTVTM; -.
DR   PhylomeDB; Q7W0S2; -.
DR   ProtClustDB; PRK05424; -.
DR   BioCyc; BPER257313:BP0011-MON; -.
DR   GO; GO:0015934; C:large 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:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   HAMAP; MF_01318_B; Ribosomal_L1_B; 1; -.
DR   InterPro; IPR005878; Ribosom_L1_bac-type.
DR   InterPro; IPR002143; Ribosomal_L1.
DR   InterPro; IPR016094; Ribosomal_L1_2-a/b-sand.
DR   InterPro; IPR016095; Ribosomal_L1_3-a/b-sand.
DR   InterPro; IPR023673; Ribosomal_L1_CS.
DR   InterPro; IPR023674; Ribosomal_L1_SF.
DR   Gene3D; G3DSA:3.30.190.20; Ribosomal_L1_2-a/b-sand; 2.
DR   Gene3D; G3DSA:3.40.50.790; Ribosomal_L1_3-a/b-sand; 1.
DR   Pfam; PF00687; Ribosomal_L1; 1.
DR   PIRSF; PIRSF002155; Ribosomal_L1; 1.
DR   SUPFAM; SSF56808; Ribosomal_L1; 1.
DR   TIGRFAMs; TIGR01169; RplA_bact; 1.
DR   PROSITE; PS01199; RIBOSOMAL_L1; 1.
DR   HOGENOMDNA; BOPER1_1.PE10; -.
KW   50S ribosomal protein L1;
KW   Complete proteome; Reference proteome; Repressor; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding; rRNA-binding; Translation regulation;
KW   tRNA-binding.
SQ   SEQUENCE   232 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAKLSKRAAA IAQKIDRTKL YPVGEALNLV KETATAKFDE SIDVAVQLGI DPKKSDQLVR
     GSVVLPAGTG KTVRVAVFAQ GEKADAARAA GADIVGLDDL AEQIKAGQMD FDVVIASPDT
     MRVVGALGQV LGPRGLMPNP KVGTVTPDVA TAVKNAKAGQ IQYRTDKAGI IHATIGRASF
     GVEQLQNNLA ALVDALQKAR PAAAKGIYLR KLAVSSTMGG GARVEIASLS AN
//

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