P0AES4

EV
Gene name
gyrA
Protein name
DNA gyrase subunit A
Names
Species
Escherichia coli (strain K12)
KEGG Pathway
eco:b2231
EC number
5.6.2.2: Enzymes altering nucleic acid conformation
Protein Class
DNA GYRASE/TOPOISOMERASE SUBUNIT A (PTHR43493)

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)

838-875 (C-terminal domain tail) EV

Target domain

531-851 (DNA gyrase domain)

Relief mechanism

Partner binding

Assay

Deletion assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

15 structures for P0AES4

Entry ID Method Resolution Chain Position Source
1AB4 X-ray 280 A A 30-522 PDB
1X75 X-ray 280 A A/B 363-494 PDB
1ZI0 X-ray 260 A A/B 535-841 PDB
2Y3P X-ray 262 A A/B 2-523 PDB
3NUH X-ray 310 A A 1-525 PDB
4ELY X-ray 193 A A/B 363-497 PDB
6RKS EM 400 A A/C 1-875 PDB
6RKU EM 400 A A/C 1-875 PDB
6RKV EM 460 A A/C 1-875 PDB
6RKW EM 660 A A/C 1-875 PDB
7Z9C EM 306 A A/C 2-875 PDB
7Z9G EM 325 A A/C 2-875 PDB
7Z9K EM 325 A A/C 2-875 PDB
7Z9M EM 330 A A/C 2-875 PDB
AF-P0AES4-F1 Predicted AlphaFoldDB

11 variants for P0AES4

Variant ID(s) Position Change Description Diseaes Association Provenance
67 A>S PPA-10; quinolone-resistant [UniProt] No
81 G>C NAL-97; quinolone-resistant [UniProt] No
83 S>L NAL-51, NAL-112, NAL-118, NAL-119 and strains 58, 158, 218, 231 and 235; quinolone-resistant [UniProt] No
83 S>W PPA-18 and strains 233 and 227; quinolone-resistant [UniProt] No
84 A>P PPA-05; quinolone-resistant [UniProt] No
87 D>N NAL-113 and OV6; quinolone-resistant [UniProt] No
87 D>V strain: 202; partially quinolone-resistant [UniProt] No
106 Q>H NAL-89; quinolone-resistant [UniProt] No
678 D>E strain: 227 [UniProt] No
798 I>IMMI strain: OV6; quinolone-resistant [UniProt] No
828 A>S strain: 227 [UniProt] No

No associated diseases with P0AES4

7 regional properties for P0AES4

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 646 - 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 PTHR43493 DNA GYRASE/TOPOISOMERASE SUBUNIT A
PANTHER Subfamily PTHR43493:SF5 DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL
PANTHER Protein Class DNA topoisomerase
PANTHER Pathway Category No pathway information available

6 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.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
DNA gyrase complex A bacterial type IIA topoisomerase that is unique in its function of introducing negative supercoils into DNA at the expense of ATP hydrolysis and is also capable of relaxing positive supercoils, an activity shared with topoisomerase IV. Typically, it is composed of two copies each of an A subunit (GyrA) and a B subunit (GyrB).
DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex Complex that possesses DNA topoisomerase II (double strand cut, ATP-hydrolyzing) activity.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.

6 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP-dependent activity, acting on DNA Catalytic activity that acts to modify DNA, driven by ATP hydrolysis.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
DNA negative supercoiling activity Catalytic introduction of negative supercoils into a DNA molecule or region thereof. In bacteria, negative supercoils are only introduced by DNA gyrase, a type II topoisomerase, but not all DNA gyrases are capable of introducing supercoils. In bacteria, the level of supercoiling varies widely between species and has been characterized properly in only a handful of organisms. The best characterized enzyme, from E.coli, is exceptionally proficient at supercoiling and this ability is not representative of all bacteria.
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.
identical protein binding Binding to an identical protein or proteins.

5 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.
negative regulation of DNA-dependent DNA replication Any process that stops, prevents, or reduces the frequency, rate or extent of DNA-dependent DNA replication.
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.
transcription, DNA-templated The synthesis of an RNA transcript from a DNA template.

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 INGCLAYIDD EDISIEGLME HIPGPDFPTA AIINGRRGIE EAYRTGRGKV
250 260 270 280 290 300
YIRARAEVEV DAKTGRETII VHEIPYQVNK ARLIEKIAEL VKEKRVEGIS ALRDESDKDG
310 320 330 340 350 360
MRIVIEVKRD AVGEVVLNNL YSQTQLQVSF GINMVALHHG QPKIMNLKDI IAAFVRHRRE
370 380 390 400 410 420
VVTRRTIFEL RKARDRAHIL EALAVALANI DPIIELIRHA PTPAEAKTAL VANPWQLGNV
430 440 450 460 470 480
AAMLERAGDD AARPEWLEPE FGVRDGLYYL TEQQAQAILD LRLQKLTGLE HEKLLDEYKE
490 500 510 520 530 540
LLDQIAELLR ILGSADRLME VIREELELVR EQFGDKRRTE ITANSADINL EDLITQEDVV
550 560 570 580 590 600
VTLSHQGYVK YQPLSEYEAQ RRGGKGKSAA RIKEEDFIDR LLVANTHDHI LCFSSRGRVY
610 620 630 640 650 660
SMKVYQLPEA TRGARGRPIV NLLPLEQDER ITAILPVTEF EEGVKVFMAT ANGTVKKTVL
670 680 690 700 710 720
TEFNRLRTAG KVAIKLVDGD ELIGVDLTSG EDEVMLFSAE GKVVRFKESS VRAMGCNTTG
730 740 750 760 770 780
VRGIRLGEGD KVVSLIVPRG DGAILTATQN GYGKRTAVAE YPTKSRATKG VISIKVTERN
790 800 810 820 830 840
GLVVGAVQVD DCDQIMMITD AGTLVRTRVS EISIVGRNTQ GVILIRTAED ENVVGLQRVA
850 860 870
EPVDEEDLDT IDGSAAEGDD EIAPEVDVDD EPEEE