P13364

PR
Gene name
gyrB
Protein name
DNA gyrase subunit B
Names
Species
Pseudomonas putida (Arthrobacter siderocapsulatus)
KEGG Pathway
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)

353-433 (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 P13364

Entry ID Method Resolution Chain Position Source
AF-P13364-F1 Predicted AlphaFoldDB

6 variants for P13364

Variant ID(s) Position Change Description Diseaes Association Provenance
161 E>D strain: JCM 6156 and PB4 [UniProt] No
245 S>N strain: JCM 6156 and PB4 [UniProt] No
249 E>D strain: JCM 6156 [UniProt] No
297 S>N strain: PB4 [UniProt] No
358 Y>F strain: PB4 [UniProt] No
360 S>A strain: JCM 6156 and PB4 [UniProt] No

No associated diseases with P13364

6 regional properties for P13364

Type Name Position InterPro Accession
domain DNA gyrase B subunit, C-terminal 579 - 640 IPR002288
domain Histidine kinase/HSP90-like ATPase 40 - 184 IPR003594
domain TOPRIM domain 429 - 543 IPR006171
domain DNA topoisomerase, type IIA, subunit B, domain 2 232 - 401 IPR013506
conserved_site DNA topoisomerase, type IIA, conserved site 433 - 441 IPR018522
domain DNA gyrase subunit B, TOPRIM domain 430 - 542 IPR034160

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

2 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.

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.

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

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSENQTYDSS SIKVLKGLDA VRKRPGMYIG DTDDGSGLHH MVFEVVDNSI DEALAGHCDD
70 80 90 100 110 120
ITVIIHTDES ISVRDNGRGI PVDVHKEEGV SAAEVIMTVL HAGGKFDDNS YKVSGGLHGV
130 140 150 160 170 180
GVSVVNALSE KLVLTVRRSG KIWEQTYVHG VPQAPMAVVG ESETTGTHIH FKPSAETFKN
190 200 210 220 230 240
IHFSWDILAK RIRELSFLNS GVGILLKDER SGKEEFFKYE GGLRAFVEYL NTNKTPVNSQ
250 260 270 280 290 300
VFHFSVQRED GVGVEVALQW NDSFNENLLC FTNNIPQRDG GTHLVGFRSS LTRSLNSYIE
310 320 330 340 350 360
QEGLAKKNKV ATTGDDAREG LTAIISVKVP DPKFSSQTKD KLVSSEVKTA VEQEMNKYFS
370 380 390 400 410 420
DFLLENPNEA KAVVGKMIDA ARAREAARKA REMTRRKGAL DIAGLPGKLA DCQEKDPALS
430 440 450 460 470 480
ELYLVEGDSA GGSAKQGRNR RTQAILPLKG KILNVEKARF DKMISSQEVG TLITALGCGI
490 500 510 520 530 540
GREEYNIDKL RYHNIIIMTD ADVDGSHIRT LLLTFFFRQL PELVERGYIY IAQPPLYKVK
550 560 570 580 590 600
KGKQEQYIKD DEAMEEYMTQ SALEDASLHL DESAPAVSGV QLESLVNEFR SVMKTLKRLS
610 620 630 640 650 660
RLYPEELTEH FVYLPEVTLE QLGDHAVMQA WLAKLQERLN SSQKSGLAYN ASLREDKERN
670 680 690 700 710 720
VWLPEVEITS HGLASYITFN RDFFGSNDYR TVVNIGAKLS SLLGEGAYVQ RGERRKAIVE
730 740 750 760 770 780
FKEGLDWLMN ETTKRHTIQR YKGLGEMNPD QLWETTMDPT VRRMLKVTIE DAIAADQIFN
790 800
TLMGDAVEPR REFIESNALS VSNLDF