Tag | Content |
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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 |
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306 | NILPRGVKLSAEDIW | acetylation | [1] | 533 | LYRIDLGKEVYYALT | acetylation | [1] | 544 | YALTEEEKEGVLEQL | acetylation | [1] | 552 | EGVLEQLKRKKGKPN | acetylation | [1] |
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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. |
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PROSITE | |
PRINTS | |