P20083

PR
Gene name
parE
Protein name
DNA topoisomerase 4 subunit B
Names
Topoisomerase IV subunit B
Species
Escherichia coli (strain K12)
KEGG Pathway
eco:b3030
EC number
5.6.2.2: Enzymes altering nucleic acid conformation
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

347-423 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

5 structures for P20083

Entry ID Method Resolution Chain Position Source
1S14 X-ray 200 A A/B 1-217 PDB
1S16 X-ray 210 A A/B 1-390 PDB
3FV5 X-ray 180 A A/B 15-215 PDB
4HZ0 X-ray 220 A A/B 12-216 PDB
AF-P20083-F1 Predicted AlphaFoldDB

1 variants for P20083

Variant ID(s) Position Change Description Diseaes Association Provenance
445 L>H strain: DH161; quinolone-resistant [UniProt] No

No associated diseases with P20083

5 regional properties for P20083

Type Name Position InterPro Accession
domain DNA gyrase B subunit, C-terminal 556 - 620 IPR002288
domain Histidine kinase/HSP90-like ATPase 27 - 173 IPR003594
domain TOPRIM domain 412 - 525 IPR006171
domain DNA topoisomerase, type IIA, subunit B, domain 2 218 - 384 IPR013506
conserved_site DNA topoisomerase, type IIA, conserved site 416 - 424 IPR018522

Functions

Description
EC Number 5.6.2.2 Enzymes altering nucleic acid conformation
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
chromosome A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex Complex that possesses DNA topoisomerase II (double strand cut, ATP-hydrolyzing) activity.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity Catalysis of a DNA topological transformation by transiently cleaving a pair of complementary DNA strands to form a gate through which a second double-stranded DNA segment is passed, after which the severed strands in the first DNA segment are rejoined, driven by ATP hydrolysis. The enzyme changes the linking number in multiples of 2.
metal ion binding Binding to a metal ion.

5 GO annotations of biological process

Name Definition
chromosome organization A process that is carried out at the cellular level that results in the assembly, arrangement of constituent parts, or disassembly of chromosomes, structures composed of a very long molecule of DNA and associated proteins that carries hereditary information. This term covers covalent modifications at the molecular level as well as spatial relationships among the major components of a chromosome.
DNA topological change The process in which a transformation is induced in the topological structure of a double-stranded DNA helix, resulting in a change in linking number.
plasmid partitioning Any process in which plasmids are segregated or distributed into daughter cells upon cell division.
response to antibiotic Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an antibiotic stimulus. An antibiotic is a chemical substance produced by a microorganism which has the capacity to inhibit the growth of or to kill other microorganisms.
sister chromatid cohesion The cell cycle process in which the sister chromatids of a replicated chromosome become tethered to each other.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTQTYNADAI EVLTGLEPVR RRPGMYTDTT RPNHLGQEVI DNSVDEALAG HAKRVDVILH
70 80 90 100 110 120
ADQSLEVIDD GRGMPVDIHP EEGVPAVELI LCRLHAGGKF SNKNYQFSGG LHGVGISVVN
130 140 150 160 170 180
ALSKRVEVNV RRDGQVYNIA FENGEKVQDL QVVGTCGKRN TGTSVHFWPD ETFFDSPRFS
190 200 210 220 230 240
VSRLTHVLKA KAVLCPGVEI TFKDEINNTE QRWCYQDGLN DYLAEAVNGL PTLPEKPFIG
250 260 270 280 290 300
NFAGDTEAVD WALLWLPEGG ELLTESYVNL IPTMQGGTHV NGLRQGLLDA MREFCEYRNI
310 320 330 340 350 360
LPRGVKLSAE DIWDRCAYVL SVKMQDPQFA GQTKERLSSR QCAAFVSGVV KDAFILWLNQ
370 380 390 400 410 420
NVQAAELLAE MAISSAQRRM RAAKKVVRKK LTSGPALPGK LADCTAQDLN RTELFLVEGD
430 440 450 460 470 480
SAGGSAKQAR DREYQAIMPL KGKILNTWEV SSDEVLASQE VHDISVAIGI DPDSDDLSQL
490 500 510 520 530 540
RYGKICILAD ADSDGLHIAT LLCALFVKHF RALVKHGHVY VALPPLYRID LGKEVYYALT
550 560 570 580 590 600
EEEKEGVLEQ LKRKKGKPNV QRFKGLGEMN PMQLRETTLD PNTRRLVQLT IDDEDDQRTD
610 620
AMMDMLLAKK RSEDRRNWLQ EKGDMAEIEV