CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004840
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA topoisomerase 4 subunit B 
Protein Synonyms/Alias
 Topoisomerase IV subunit B 
Gene Name
 parE 
Gene Synonyms/Alias
 nfxD; b3030; JW2998 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
306NILPRGVKLSAEDIWacetylation[1]
533LYRIDLGKEVYYALTacetylation[1]
544YALTEEEKEGVLEQLacetylation[1]
552EGVLEQLKRKKGKPNacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618
Functional Description
 Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule. MukB stimulates the relaxation activity of topoisomerase IV and also has a modest effect on decatenation. 
Sequence Annotation
 DOMAIN 412 525 Toprim.
 NP_BIND 110 116 ATP.
 METAL 418 418 Magnesium 1; catalytic (By similarity).
 METAL 490 490 Magnesium 1; catalytic (By similarity).
 METAL 490 490 Magnesium 2 (By similarity).
 METAL 492 492 Magnesium 2 (By similarity).
 BINDING 5 5 ATP.
 BINDING 42 42 ATP.
 BINDING 69 69 ATP.
 BINDING 334 334 ATP.  
Keyword
 3D-structure; Antibiotic resistance; ATP-binding; Complete proteome; DNA-binding; Isomerase; Magnesium; Metal-binding; Nucleotide-binding; Reference proteome; Topoisomerase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 630 AA 
Protein Sequence
MTQTYNADAI EVLTGLEPVR RRPGMYTDTT RPNHLGQEVI DNSVDEALAG HAKRVDVILH 60
ADQSLEVIDD GRGMPVDIHP EEGVPAVELI LCRLHAGGKF SNKNYQFSGG LHGVGISVVN 120
ALSKRVEVNV RRDGQVYNIA FENGEKVQDL QVVGTCGKRN TGTSVHFWPD ETFFDSPRFS 180
VSRLTHVLKA KAVLCPGVEI TFKDEINNTE QRWCYQDGLN DYLAEAVNGL PTLPEKPFIG 240
NFAGDTEAVD WALLWLPEGG ELLTESYVNL IPTMQGGTHV NGLRQGLLDA MREFCEYRNI 300
LPRGVKLSAE DIWDRCAYVL SVKMQDPQFA GQTKERLSSR QCAAFVSGVV KDAFILWLNQ 360
NVQAAELLAE MAISSAQRRM RAAKKVVRKK LTSGPALPGK LADCTAQDLN RTELFLVEGD 420
SAGGSAKQAR DREYQAIMPL KGKILNTWEV SSDEVLASQE VHDISVAIGI DPDSDDLSQL 480
RYGKICILAD ADSDGLHIAT LLCALFVKHF RALVKHGHVY VALPPLYRID LGKEVYYALT 540
EEEKEGVLEQ LKRKKGKPNV QRFKGLGEMN PMQLRETTLD PNTRRLVQLT IDDEDDQRTD 600
AMMDMLLAKK RSEDRRNWLQ EKGDMAEIEV 630 
Gene Ontology
 GO:0005694; C:chromosome; IEA:InterPro.
 GO:0009295; C:nucleoid; IBA:RefGenome.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IBA:RefGenome.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006265; P:DNA topological change; IBA:RefGenome.
 GO:0006261; P:DNA-dependent DNA replication; IBA:RefGenome.
 GO:0030541; P:plasmid partitioning; IDA:EcoliWiki.
 GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
 GO:0007062; P:sister chromatid cohesion; IMP:EcoliWiki. 
Interpro
 IPR002288; DNA_gyrase_B_C.
 IPR003594; HATPase_ATP-bd.
 IPR020568; Ribosomal_S5_D2-typ_fold.
 IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
 IPR001241; Topo_IIA.
 IPR013506; Topo_IIA_bsu_dom2.
 IPR013759; Topo_IIA_cen_dom.
 IPR013760; Topo_IIA_like_dom.
 IPR018522; TopoIIA_CS.
 IPR005737; TopoIV_B_Gneg.
 IPR006171; Toprim_domain. 
Pfam
 PF00204; DNA_gyraseB
 PF00986; DNA_gyraseB_C
 PF02518; HATPase_c
 PF01751; Toprim 
SMART
 SM00387; HATPase_c
 SM00433; TOP2c 
PROSITE
 PS00177; TOPOISOMERASE_II
 PS50880; TOPRIM 
PRINTS
 PR00418; TPI2FAMILY.