Q5HG65

PR
Gene name
parE
Protein name
DNA topoisomerase 4 subunit B
Names
Topoisomerase IV subunit B
Species
Staphylococcus aureus (strain COL)
KEGG Pathway
sac:SACOL1389
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)

1-111 (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 Q5HG65

Entry ID Method Resolution Chain Position Source
AF-Q5HG65-F1 Predicted AlphaFoldDB

No variants for Q5HG65

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5HG65

No associated diseases with Q5HG65

5 regional properties for Q5HG65

Type Name Position InterPro Accession
domain DNA gyrase B subunit, C-terminal 570 - 631 IPR002288
domain Histidine kinase/HSP90-like ATPase 32 - 176 IPR003594
domain TOPRIM domain 424 - 538 IPR006171
domain DNA topoisomerase, type IIA, subunit B, domain 2 224 - 394 IPR013506
conserved_site DNA topoisomerase, type IIA, conserved site 428 - 436 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
MNKQNNYSDD SIQVLEGLEA VRKRPGMYIG STDKRGLHHL VYEIVDNSVD EVLNGYGNEI
70 80 90 100 110 120
DVTINKDGSI SIEDNGRGMP TGIHKSGKPT VEVIFTVLHA GGKFGQGGYK TSGGLHGVGA
130 140 150 160 170 180
SVVNALSEWL EVEIHRDGNI YHQSFKNGGS PSSGLVKKGK TKKTGTKVTF KPDDTIFKAS
190 200 210 220 230 240
TSFNFDVLSE RLQESAFLLK NLKITLNDLR SGKERQEHYH YEEGIKEFVS YVNEGKEVLH
250 260 270 280 290 300
DVATFSGEAN GIEVDVAFQY NDQYSESILS FVNNVRTKDG GTHEVGFKTA MTRVFNDYAR
310 320 330 340 350 360
RINELKTKDK NLDGNDIREG LTAVVSVRIP EELLQFEGQT KSKLGTSEAR SAVDSVVADK
370 380 390 400 410 420
LPFYLEEKGQ LSKSLVKKAI KAQQAREAAR KAREDARSGK KNKRKDTLLS GKLTPAQSKN
430 440 450 460 470 480
TEKNELYLVE GDSAGGSAKL GRDRKFQAIL PLRGKVINTE KARLEDIFKN EEINTIIHTI
490 500 510 520 530 540
GAGVGTDFKI EDSNYNRVII MTDADTDGAH IQVLLLTFFF KYMKPLVQAG RVFIALPPLY
550 560 570 580 590 600
KLEKGKGKTK RVEYAWTDEE LNKLQKELGK GFTLQRYKGL GEMNPEQLWE TTMNPETRTL
610 620 630 640 650 660
IRVQVEDEVR SSKRVTTLMG DKVQPRREWI EKHVEFGMQE DQSILDNSEV QVLENDQFDE
EEI