(data stored in ACNUC15324 zone)

HOGENOM: ACIBY_5_PE120

ID   ACIBY_5_PE120                        STANDARD;      PRT;   627 AA.
AC   ACIBY_5_PE120; B0V9T6;
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   SubName: Full=Topoisomerase IV subunit B; EC=5.99.1 -; (ACIBY_5.PE120).
GN   Name=parE; OrderedLocusNames=ABAYE0126;
OS   ACINETOBACTER BAUMANNII AYE.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter; Acinetobacter calcoaceticus/baumannii
OC   complex.
OX   NCBI_TaxID=509173;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACIBY_5.PE120.
CC       Acinetobacter baumannii AYE, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:B0V9T6_ACIBY
CC   -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC   -!- GENE_FAMILY: HOG000075154 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B0V9T6; -.
DR   EMBL; CU459141; CAM85112.1; -; Genomic_DNA.
DR   RefSeq; YP_001712119.1; NC_010410.1.
DR   PDB; 2XKJ; X-ray; 2.20 A; E=370-627.
DR   PDB; 2XKK; X-ray; 3.25 A; A/C=370-627.
DR   PDBsum; 2XKJ; -.
DR   PDBsum; 2XKK; -.
DR   ProteinModelPortal; B0V9T6; -.
DR   SMR; B0V9T6; 4-383.
DR   STRING; B0V9T6; -.
DR   GeneID; 6000336; -.
DR   GenomeReviews; CU459141_GR; ABAYE0126.
DR   OMA; QARDKEF; -.
DR   ProtClustDB; PRK05559; -.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003918; F:DNA topoisomerase (ATP-hydrolyzing) activity; IEA:InterPro.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   InterPro; IPR003594; ATPase-like_ATP-bd.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR001241; Topo_IIA_B/N.
DR   InterPro; IPR013759; Topo_IIA_B/N_ab.
DR   InterPro; IPR002288; Topo_IIA_B_C.
DR   InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR   InterPro; IPR013760; Topo_IIA_cen.
DR   InterPro; IPR018522; TopoIIA_CS.
DR   InterPro; IPR005737; TopoIV_B_Gneg.
DR   Gene3D; G3DSA:3.30.565.10; ATP_bd_ATPase; 1.
DR   Gene3D; G3DSA:3.30.230.10; Ribosomal_S5_D2-type_fold; 1.
DR   Gene3D; G3DSA:3.40.50.670; Topo_IIA_B/N_ab; 1.
DR   Pfam; PF00204; DNA_gyraseB; 1.
DR   Pfam; PF00986; DNA_gyraseB_C; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   PRINTS; PR00418; TPI2FAMILY.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00433; TOP2c; 1.
DR   SUPFAM; SSF55874; ATP_bd_ATPase; 1.
DR   SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1.
DR   SUPFAM; SSF56719; Topo_IIA_cen; 1.
DR   TIGRFAMs; TIGR01055; ParE_Gneg; 1.
DR   PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR   HOGENOMDNA; ACIBY_5.PE120; -.
KW   3D-structure; ATP-binding; Complete proteome; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   627 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTQYTAQSLE VLSGLDPVRR RPGMYTDTSR PNHLAQEVID NAVDEALAGH ADKICVTVYK
     DGSLSVEDNG RGMPVDIHPE YGQSGIEIIL TKLHAGGKFS TDNYQFSGGL HGVGISVVNA
     LSTRVEVEVQ RQGNLYQMAF EQGEPVAPLA VLEGKAPKRA TGTTVRFWPE AKYFDSPKFA
     LKALKHNLKA KAVLAAGLKI TYIDQINDEK IEWQFENGLV DYLMDELQDR EILPNPAFVS
     SGQADRAACE FAICWNVEGG EQVQESYVNL IPTAQGGTHV NGLRSGVTEA LREFCELRNL
     LPRNLKLSAE DVWDGVNYIL SLKFQEPQFS GQTKERLSSR EAANIVLNIA KDAFALWLNQ
     HAEIAMQLAE MAISKAGRRL KAAKKVERKK IVSGPALPGK LADCVGQTRE ESELFIVEGD
     SAGGSAKQAR DKNFQAIMPI RGKILNTWEV SSDEVLASQE VHDIAIAIGV DPGSDDLSEL
     RYGKICILAD ADSDGLHIAT LLCALFVKHF PALVEEGHLY VAMPPLFRID IGKDVHYALD
     DEELETILKN VKGNKNPQIT RFKGLGEMNA IQLRETTMDP NTRRLVQLDL DDAHLTAGLL
     DKLLAKKRAA DRKQWLEQKG NLADITV
//

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