Q59192

PR
Gene name
parE
Protein name
DNA topoisomerase 4 subunit B
Names
Topoisomerase IV subunit B
Species
Bacillus subtilis (strain 168)
KEGG Pathway
bsu:BSU18090
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)

349-442 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q59192

Entry ID Method Resolution Chain Position Source
AF-Q59192-F1 Predicted AlphaFoldDB

No variants for Q59192

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q59192

No associated diseases with Q59192

5 regional properties for Q59192

Type Name Position InterPro Accession
domain DNA gyrase B subunit, C-terminal 569 - 630 IPR002288
domain Histidine kinase/HSP90-like ATPase 34 - 178 IPR003594
domain TOPRIM domain 423 - 537 IPR006171
domain DNA topoisomerase, type IIA, subunit B, domain 2 223 - 393 IPR013506
conserved_site DNA topoisomerase, type IIA, conserved site 427 - 435 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

1 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.

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.

2 GO annotations of biological process

Name Definition
chromosome segregation The process in which genetic material, in the form of chromosomes, is organized into specific structures and then physically separated and apportioned to two or more sets. In eukaryotes, chromosome segregation begins with the condensation of chromosomes, includes chromosome separation, and ends when chromosomes have completed movement to the spindle poles.
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MARKQQFDYN EDAIQVLEGL EAVRKRPGMY IGSTDARGLH HLVYEIVDNS VDEVLAGHGD
70 80 90 100 110 120
HIIVKIHKDN SISVQDRGRG MPTGMHKLGK PTPEVILTVL HAGGKFGQGG YKTSGGLHGV
130 140 150 160 170 180
GASVVNALSE WLTVTIERDG FVYQQRFENG GKPVTSLEKI GKTKKTGTLT HFKPDPTMFS
190 200 210 220 230 240
TTTYNFETLS ERLRESAFLL KGLKIELIDE RNDQREVFYY ENGIEAFVAY LNEEKDVLSE
250 260 270 280 290 300
VVSFEGEHHS IEVDFAFQFN DGYSENILSF VNNVRTKDGG THESGAKTAM TRAFNEYARK
310 320 330 340 350 360
VALLKEKDKN LEGTDIREGL SAIISVRIPE ELLQFEGQTK GKLGTSEARS AVDAIVSEQL
370 380 390 400 410 420
AYFLEENRDT ATLLVKKAIK ASQAREAARK AREEARSGKK RKKSEATLSG KLTPAGSRNP
430 440 450 460 470 480
AKNELYLVEG DSAGGSAKQG RDRRFQAVLP LRGKVINTEK AKLADIFKNE EINTIIHAIG
490 500 510 520 530 540
GGVGADFSID DINYDKIIIM TDADTDGAHI QVLLLTFFYR YMKPLIEHGK VFIALPPLYK
550 560 570 580 590 600
VSKGSGKKEI IEYAWSDEEM GDVLKKVGKG YTIQRYKGLG EMNADQLWET TMNPESRTLV
610 620 630 640 650
RVKIDDAARV ERRVTTLMGD KVEPRRKWIE KNVAFGLDEE SNILENENLS VAEEV