Descriptions

Gyrase, a prokaryotic type IIA topoisomerase, consumes ATP to introduce negative supercoils through a strand passage mechanism. The removal of either the entirety or an internal portion of the acidic tail at the extreme C terminus of the Escherichia coli GyrA CTD bestows GyrA with the capacity to wrap DNA to increase the coupling efficiency between ATP turnover and supercoiling, whereas the full-length GyrA CTD is unable to wrap, or even bind DNA.

Autoinhibitory domains (AIDs)

Target domain

538-839 (DNA gyrase domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for P37411

Entry ID Method Resolution Chain Position Source
AF-P37411-F1 Predicted AlphaFoldDB

No variants for P37411

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P37411

No associated diseases with P37411

7 regional properties for P37411

Type Name Position InterPro Accession
domain DNA topoisomerase, type IIA, domain A 11 - 507 IPR002205
repeat DNA gyrase/topoisomerase IV, subunit A, C-terminal repeat 538 - 584 IPR006691-1
repeat DNA gyrase/topoisomerase IV, subunit A, C-terminal repeat 588 - 637 IPR006691-2
repeat DNA gyrase/topoisomerase IV, subunit A, C-terminal repeat 645 - 688 IPR006691-3
repeat DNA gyrase/topoisomerase IV, subunit A, C-terminal repeat 692 - 737 IPR006691-4
repeat DNA gyrase/topoisomerase IV, subunit A, C-terminal repeat 744 - 789 IPR006691-5
repeat DNA gyrase/topoisomerase IV, subunit A, C-terminal repeat 793 - 839 IPR006691-6

Functions

Description
EC Number 5.6.2.2 Enzymes altering nucleic acid conformation
Subcellular Localization
  • Cytoplasm
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.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex Complex that possesses DNA topoisomerase II (double strand cut, ATP-hydrolyzing) activity.

3 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.

2 GO annotations of biological process

Name Definition
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.
DNA-dependent DNA replication A DNA replication process that uses parental DNA as a template for the DNA-dependent DNA polymerases that synthesize the new strands.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSDLAREITP VNIEEELKSS YLDYAMSVIV GRALPDVRDG LKPVHRRVLY AMNVLGNDWN
70 80 90 100 110 120
KAYKKSARVV GDVIGKYHPH GDSAVYDTIV RMAQPFSLRY MLVDGQGNFG SIDGDSAAAM
130 140 150 160 170 180
RYTEIRLAKI AHELMADLEK ETVDFVDNYD GTEKIPDVMP TKIPNLLVNG SSGIAVGMAT
190 200 210 220 230 240
NIPPHNLTEV INGCLAYIDN EDISIEGLME HIPGPDFPTA AIINGRRGIE EAYRTGRGKV
250 260 270 280 290 300
YIRARAEVEA DAKTGRETII VHEIPYQVNK ARLIEKIAEL VKDKRVEGIS ALRDESDKDG
310 320 330 340 350 360
MRIVIEVKRD AVGEVVLNNL YSQTQLQVSF GINMVALHHG QPKIMNLKDI ISAFVRHRRE
370 380 390 400 410 420
VVTRRTIFEL RKARDRAHIL EALAIALANI DPIIELIRRA PTPAEAKAAL ISRPWDLGNV
430 440 450 460 470 480
AAMLERAGDD AARPEWLEPE FGVRDGQYYL TEQQAQAILD LRLQKLTGLE HEKLLDEYKE
490 500 510 520 530 540
LLEQIAELLH ILGSADRLME VIREEMELIR DQFGDERRTE ITANSADINI EDLISQEDVV
550 560 570 580 590 600
VTLSHQGYVK YQPLTDYEAQ RRGGKGKSAA RIKEEDFIDR LLVANTHDTI LCFSSRGRLY
610 620 630 640 650 660
WMKVYQLPEA SRGARGRPIV NLLPLEANER ITAILPVREY EEGVNVFMAT ASGTVKKTAL
670 680 690 700 710 720
TEFSRPRSAG IIAVNLNDGD ELIGVDLTSG SDEVMLFSAA GKVVRFKEDA VRAMGRTATG
730 740 750 760 770 780
VRGIKLAGDD KVVSLIIPRG EGAILTVTQN GYGKRTAADE YPTKSRATQG VISIKVTERN
790 800 810 820 830 840
GSVVGAVQVD DCDQIMMITD AGTLVRTRVS EISVVGRNTQ GVILIRTAED ENVVGLQRVA
850 860 870
EPVDDEELDA IDGSVAEGDE DIAPEAESDD DVADDADE