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Protein

DNA gyrase subunit B

Gene

gyrB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

DNA gyrase negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner to maintain chromosomes in an underwound state (PubMed:186775, PubMed:3031051, PubMed:1323022, PubMed:8248233, PubMed:7811004, PubMed:8621650, PubMed:9657678, PubMed:12051842, PubMed:12051843, PubMed:18642932, PubMed:19060136, PubMed:19965760, PubMed:22457353, PubMed:23294697, PubMed:20356737, PubMed:20675723, PubMed:23352267, PubMed:24386374, PubMed:25202966, PubMed:25849408). This makes better substrates for topoisomerase 4 (ParC and ParE) which is the main enzyme that unlinks newly replicated chromosomes in E.coli (PubMed:9334322). Gyrase catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes (PubMed:22457352). Relaxes negatively supercoiled DNA in an ATP-independent manner (PubMed:337300). E.coli gyrase has higher supercoiling activity than other characterized bacterial gyrases; at comparable concentrations E.coli gyrase introduces more supercoils faster than M.tuberculosis gyrase, while M.tuberculosis gyrase has higher decatenation than supercoiling activity compared to E.coli (PubMed:22457352). E.coli makes 15% more negative supercoils in pBR322 plasmid DNA than S.typhimurium; the S.typhimurium GyrB subunit is toxic in E.coli, while the E.coli copy can be expressed in S.typhimurium even though the 2 subunits have 777/804 residues identical (PubMed:17400739). The enzymatic differences between E.coli gyrase and topoisomerase IV are largely due to the GyrA C-terminal domain (approximately residues 524-841) and specifically the GyrA-box (PubMed:8962066, PubMed:16332690).27 Publications

Miscellaneous

When the enzyme transiently cleaves DNA a phosphotyrosine bond is formed between GyrA and DNA in an ATP-independent manner (PubMed:3031051). In the presence of quinolones this intermediate can be trapped and is used as an indicator of drug toxicity (PubMed:12051842).1 Publication1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Gyrase is the target of many classes of inhibitors, including coumarins, cyclothialidines, pyrrolopyrimidines, pyrazolthiazoles and (fluoro)quinolones. Coumarins bind to GyrB and are competitive inhibitors of its ATPase activity (PubMed:7811004). Cyclothialidines also bind GyrB and are ATPase competitive inhibitors; they seem to act differently from coumarins (PubMed:7811004, PubMed:8635474). Pyrrolopyrimidines inhibit both GyrB and its paralog in topoisomerase 4 (parE) (PubMed:23294697, PubMed:23352267, PubMed:24386374). Pyrazolthiazoles also inhibit the ATPase activity of GyrB (PubMed:20356737). Quinolones bind GyrA when the enzyme is complexed with DNA and trap the enzyme in a covalent reaction intermediate with DNA (PubMed:3031051, PubMed:12051842, PubMed:337300). Acriflavine inhibits DNA supercoiling and DNA-stimulated ATPase activity (PubMed:9148951). DNA supercoiling activity is protected from fluoroquinolone inhibition by QnrB4; QnrB4 has no effect on supercoiling activity alone (PubMed:19060136).1 Publication10 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei5ATP1 Publication2 Publications1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei42Proton acceptor (ATPase activity)2 Publications1
Binding sitei46ADP3 Publications1
Binding sitei73ATP3 Publications1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi94Potassium; via carbonyl oxygen1 Publication1
Metal bindingi97Potassium; via carbonyl oxygen1 Publication1
Metal bindingi100Potassium; via carbonyl oxygen1 Publication1
Metal bindingi103Sodium1 Publication1
Metal bindingi105Sodium1 Publication1
Binding sitei109ATP3 Publications1
Metal bindingi117Potassium; via carbonyl oxygen1 Publication1
Metal bindingi121Potassium1 Publication1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei337Transition state stabilizer1 Publication1
Metal bindingi424Magnesium 1; catalyticUniRule annotation2 Publications1
Metal bindingi498Magnesium 1; catalyticUniRule annotation2 Publications1
Metal bindingi498Magnesium 2UniRule annotation2 Publications1
Metal bindingi500Magnesium 2UniRule annotation2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi102 – 103ATP3 Publications2
Nucleotide bindingi115 – 120ATP3 Publications6
Nucleotide bindingi335 – 337ATP2 Publications3

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

  • DNA-dependent DNA replication Source: UniProtKB-UniRule
  • DNA topological change Source: EcoliWiki
  • response to antibiotic Source: UniProtKB-KW
  • response to drug Source: EcoliWiki
  • transcription, DNA-templated Source: EcoliWiki

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding, Isomerase, Topoisomerase
Biological processAntibiotic resistance
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Sodium

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG10424-MONOMER
MetaCyc:EG10424-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
5.99.1.3 2026

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
DNA gyrase subunit BUniRule annotation (EC:5.99.1.3UniRule annotation5 Publications)
Alternative name(s):
Type IIA topoisomerase subunit GyrB
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:gyrBUniRule annotation
Synonyms:acrB1 Publication, cou, himB, hisU, nalC, parA, pcbA
Ordered Locus Names:b3699, JW5625
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10424 gyrB

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1 – 14Missing : No dimerization of residues 15-393, fragment has no ATPase activity. 1 PublicationAdd BLAST14
Mutagenesisi5Y → F or S: 5- to 10-fold reduced dimerization of residues 2-393, fragment has 3- to 5-fold reduced ATPase activity. Fragment dimerizes upon crystallization. 1 Publication1
Mutagenesisi10I → G: No dimerization of residues 2-393, fragment has significantly decreased ATPase activity. 1 Publication1
Mutagenesisi38H → A: 0.2% supercoiling activity, 7% DNA-dependent ATPase activity, binds ATP normally, complements the N4177 ts mutant. 1 Publication1
Mutagenesisi42E → A: No supercoiling or DNA-dependent ATPase activity, 25% fluoroquinolone-induced DNA cleavage, 50% ATP-independent DNA relaxation, binds ATP normally, does not complement the N4177 ts mutant. 1 Publication1
Mutagenesisi42E → D: 7% supercoiling activity, 16% DNA-dependent ATPase activity, fluoroquinolone-induced DNA cleavage normal, 40% ATP-independent DNA relaxation, binds ATP normally, complements the N4177 ts mutant. 1 Publication1
Mutagenesisi42E → Q: No supercoiling or DNA-dependent ATPase activity, binds ATP normally, does not complement the N4177 ts mutant. 1 Publication1
Mutagenesisi103K → E, I or T: Retains ATP-independent DNA relaxation and quinolone-induced DNA cleavage; loss of supercoiling activity, loss of ATPase, does not bind ATP analogs. 1 Publication1
Mutagenesisi110K → E or V: Binds about 50% ATP analog, 2- to 3-fold decreased ATPase, retains ATP-independent DNA relaxation, quinolone-induced DNA cleavage and negative supercoiling activity. 1 Publication1
Mutagenesisi136R → C, H or S: Resistance to coumarin antibiotics, decreased ATPase and DNA supercoiling. 1 Publication1
Mutagenesisi164G → V: Resistance to coumarin antibiotics, decreased ATPase and DNA supercoiling. 1 Publication1
Mutagenesisi335Q → A: Wild-type ATP analog-binding and ATPase activity in N-terminal fragment GyrB43 (residues 2-393), in whole protein wild-type DNA supercoiling and ATP-independent DNA relaxation, 50% ATPase activity which is not stimulated by DNA, complements the N4177 ts mutant. 1 Publication1
Mutagenesisi337K → Q: Binds about 60% ATP analog but strongly decreased enzyme turnover for ATPase activity in N-terminal fragment GyrB43 (residues 2-393), in whole protein <1% DNA supercoiling and ATPase activity not stimulated by DNA, wild-type ATP-independent DNA relaxation and quinolone-induced DNA cleavage, does not complement the N4177 ts mutant. 1 Publication1
Mutagenesisi424E → A or Q: Strongly reduced DNA supercoiling and relaxation activity. Reduces ATP hydrolysis in response to DNA binding, but has only minor effect on the basal rate of ATP hydrolysis. 1 Publication1
Mutagenesisi436R → S: Cannot be made, suggesting it is lethal. This is temperature-sensitive in S.typhimurium, but not lethal. 1 Publication1
Mutagenesisi498D → A or N: Strongly reduced DNA supercoiling and relaxation activity. Reduces ATP hydrolysis in response to DNA binding, but has only minor effect on the basal rate of ATP hydrolysis. 1 Publication1
Mutagenesisi500D → A: Strongly reduced DNA supercoiling and relaxation activity. Reduces ATP hydrolysis in response to DNA binding, but has only minor effect on the basal rate of ATP hydrolysis. 1 Publication1
Mutagenesisi500D → C or H: Alters metal-dependency of ATP-independent DNA relaxation, prefers Mn(2+) and Co(2+) over wild-type Mg(2+). 1 Publication1
Mutagenesisi502D → A: Strongly reduced DNA supercoiling and relaxation activity. Reduces ATP hydrolysis in response to DNA binding, but has only minor effect on the basal rate of ATP hydrolysis. 1 Publication1
Mutagenesisi502D → C or H: Alters metal-dependency of ATP-independent DNA relaxation, prefers Mn(2+) and Co(2+) over wild-type Mg(2+). 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1826

Drug and drug target database

More...
DrugBanki
DB05488 99mTc-ciprofloxacin
DB03966 Clorobiocin
DB04395 Phosphoaminophosphonic Acid-Adenylate Ester
DB00817 Rosoxacin

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001453092 – 804DNA gyrase subunit BAdd BLAST803

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P0AES6

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P0AES6

PRoteomics IDEntifications database

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PRIDEi
P0AES6

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heterotetramer, composed of two GyrA and two GyrB chains (PubMed:9148951, PubMed:12051842). In the heterotetramer, GyrA contains the active site tyrosine that forms a transient covalent intermediate with the DNA, while GyrB binds cofactors and catalyzes ATP hydrolysis (PubMed:12051843, PubMed:18642932, PubMed:20675723, PubMed:19965760).UniRule annotation6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei449Interaction with DNAUniRule annotation1
Sitei452Interaction with DNAUniRule annotation1

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
gyrAP0AES47EBI-541911,EBI-547129

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
4259537, 175 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-2177 GyrA-GyrB complex

Database of interacting proteins

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DIPi
DIP-48005N

Protein interaction database and analysis system

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IntActi
P0AES6, 20 interactors

STRING: functional protein association networks

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STRINGi
316407.85676345

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P0AES6

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1804
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P0AES6

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P0AES6

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P0AES6

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini418 – 533ToprimUniRule annotationAdd BLAST116

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2 – 220ATPase domain2 PublicationsAdd BLAST219
Regioni221 – 392Transducer domain2 PublicationsAdd BLAST172

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Consists of 3 domains; the ATPase domain (residues 1-220), the transducer domain (221-392) and the toprim domain (393-804) (PubMed:1646964, PubMed:10734094). ATP-binding is cooperative, and both subunits must be wild-type at residue 103 for supercoiling to occur (PubMed:8621650). Non-hydrolyzable ATP analogs (and ATP-binding) induce dimerization and enhance ATPase activity (PubMed:10734094, PubMed:9657678). ATP hydrolysis induces domain shifts that are probably part of the mechanism of DNA cleavage and rejoining (PubMed:25202966).2 Publications3 Publications

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the type II topoisomerase family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG4105C7D Bacteria
COG0187 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000075155

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P0AES6

KEGG Orthology (KO)

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KOi
K02470

Database for complete collections of gene phylogenies

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PhylomeDBi
P0AES6

Family and domain databases

Conserved Domains Database

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CDDi
cd00075 HATPase_c, 1 hit
cd03366 TOPRIM_TopoIIA_GyrB, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.230.10, 1 hit
3.30.565.10, 1 hit
3.40.50.670, 2 hits

HAMAP database of protein families

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HAMAPi
MF_01898 GyrB, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR002288 DNA_gyrase_B_C
IPR011557 GyrB
IPR003594 HATPase_C
IPR036890 HATPase_C_sf
IPR020568 Ribosomal_S5_D2-typ_fold
IPR014721 Ribosomal_S5_D2-typ_fold_subgr
IPR001241 Topo_IIA
IPR013760 Topo_IIA-like_dom_sf
IPR013759 Topo_IIA_B_C
IPR013506 Topo_IIA_bsu_dom2
IPR018522 TopoIIA_CS
IPR006171 TOPRIM_domain
IPR034160 TOPRIM_GyrB

The PANTHER Classification System

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PANTHERi
PTHR10169 PTHR10169, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00204 DNA_gyraseB, 1 hit
PF00986 DNA_gyraseB_C, 1 hit
PF02518 HATPase_c, 1 hit
PF01751 Toprim, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00387 HATPase_c, 1 hit
SM00433 TOP2c, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF54211 SSF54211, 1 hit
SSF55874 SSF55874, 1 hit
SSF56719 SSF56719, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR01059 gyrB, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00177 TOPOISOMERASE_II, 1 hit
PS50880 TOPRIM, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P0AES6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSNSYDSSSI KVLKGLDAVR KRPGMYIGDT DDGTGLHHMV FEVVDNAIDE
60 70 80 90 100
ALAGHCKEII VTIHADNSVS VQDDGRGIPT GIHPEEGVSA AEVIMTVLHA
110 120 130 140 150
GGKFDDNSYK VSGGLHGVGV SVVNALSQKL ELVIQREGKI HRQIYEHGVP
160 170 180 190 200
QAPLAVTGET EKTGTMVRFW PSLETFTNVT EFEYEILAKR LRELSFLNSG
210 220 230 240 250
VSIRLRDKRD GKEDHFHYEG GIKAFVEYLN KNKTPIHPNI FYFSTEKDGI
260 270 280 290 300
GVEVALQWND GFQENIYCFT NNIPQRDGGT HLAGFRAAMT RTLNAYMDKE
310 320 330 340 350
GYSKKAKVSA TGDDAREGLI AVVSVKVPDP KFSSQTKDKL VSSEVKSAVE
360 370 380 390 400
QQMNELLAEY LLENPTDAKI VVGKIIDAAR AREAARRARE MTRRKGALDL
410 420 430 440 450
AGLPGKLADC QERDPALSEL YLVEGDSAGG SAKQGRNRKN QAILPLKGKI
460 470 480 490 500
LNVEKARFDK MLSSQEVATL ITALGCGIGR DEYNPDKLRY HSIIIMTDAD
510 520 530 540 550
VDGSHIRTLL LTFFYRQMPE IVERGHVYIA QPPLYKVKKG KQEQYIKDDE
560 570 580 590 600
AMDQYQISIA LDGATLHTNA SAPALAGEAL EKLVSEYNAT QKMINRMERR
610 620 630 640 650
YPKAMLKELI YQPTLTEADL SDEQTVTRWV NALVSELNDK EQHGSQWKFD
660 670 680 690 700
VHTNAEQNLF EPIVRVRTHG VDTDYPLDHE FITGGEYRRI CTLGEKLRGL
710 720 730 740 750
LEEDAFIERG ERRQPVASFE QALDWLVKES RRGLSIQRYK GLGEMNPEQL
760 770 780 790 800
WETTMDPESR RMLRVTVKDA IAADQLFTTL MGDAVEPRRA FIEENALKAA

NIDI
Length:804
Mass (Da):89,950
Last modified:January 23, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD831B95FFB3A7EE3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti385A → P in AAA62050 (PubMed:7686882).Curated1
Sequence conflicti436R → G in BAA20341 (PubMed:9148951).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti426D → N in nal-24, nal-102, nal-103, nal-107, nal-108, nal-111, nal-114, en-2 and en-5 mutants; resistant to nalidixic acid and to enoxacin. 1 Publication1
Natural varianti447K → E in nal-31, nal-109, nal-115 and nal-120 mutants; resistant to nalidixic acid. 1 Publication1
Natural varianti751W → R in microcin B17 resistant mutant. 1 Publication1
Natural varianti759 – 760SR → RC in acriflavine susceptible mutant acrB, decreased supercoiling activity, ATPase activity no longer stimulated by DNA, decreased DNA-binding, bind GyrA normally. 1 Publication2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X04341 Genomic DNA Translation: CAA27871.1
D87842 Genomic DNA Translation: BAA20341.1
L10328 Genomic DNA Translation: AAA62050.1
U00096 Genomic DNA Translation: AAT48201.1
AP009048 Genomic DNA Translation: BAE77595.1
M15548 Genomic DNA Translation: AAA23949.1

Protein sequence database of the Protein Information Resource

More...
PIRi
D65172 ISECTB

NCBI Reference Sequences

More...
RefSeqi
WP_000072067.1, NZ_LN832404.1
YP_026241.1, NC_000913.3

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAT48201; AAT48201; b3699
BAE77595; BAE77595; BAE77595

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
948211

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW5625
eco:b3699

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|511145.12.peg.3823

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04341 Genomic DNA Translation: CAA27871.1
D87842 Genomic DNA Translation: BAA20341.1
L10328 Genomic DNA Translation: AAA62050.1
U00096 Genomic DNA Translation: AAT48201.1
AP009048 Genomic DNA Translation: BAE77595.1
M15548 Genomic DNA Translation: AAA23949.1
PIRiD65172 ISECTB
RefSeqiWP_000072067.1, NZ_LN832404.1
YP_026241.1, NC_000913.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AJ6X-ray2.30A2-220[»]
1EI1X-ray2.30A/B2-392[»]
1KZNX-ray2.30A15-219[»]
3G7EX-ray2.20A15-217[»]
3NUHX-ray3.10B389-804[»]
4DUHX-ray1.50A/B1-220[»]
4HYPX-ray2.60A/B/C/D15-220[»]
4KFGX-ray1.60A/B15-220[»]
4PRVX-ray2.00A2-392[»]
4PRXX-ray1.80A2-392[»]
4PU9X-ray2.40A2-392[»]
4WUBX-ray1.75A2-393[»]
4WUCX-ray1.90A2-393[»]
4WUDX-ray1.95A2-393[»]
4XTJX-ray1.92A2-392[»]
4ZVIX-ray2.20A16-392[»]
5L3JX-ray2.83A15-392[»]
5MMNX-ray1.90A1-220[»]
5MMOX-ray1.81A1-220[»]
5MMPX-ray2.05A1-220[»]
ProteinModelPortaliP0AES6
SMRiP0AES6
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259537, 175 interactors
ComplexPortaliCPX-2177 GyrA-GyrB complex
DIPiDIP-48005N
IntActiP0AES6, 20 interactors
STRINGi316407.85676345

Chemistry databases

BindingDBiP0AES6
ChEMBLiCHEMBL1826
DrugBankiDB05488 99mTc-ciprofloxacin
DB03966 Clorobiocin
DB04395 Phosphoaminophosphonic Acid-Adenylate Ester
DB00817 Rosoxacin

Proteomic databases

EPDiP0AES6
PaxDbiP0AES6
PRIDEiP0AES6

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT48201; AAT48201; b3699
BAE77595; BAE77595; BAE77595
GeneIDi948211
KEGGiecj:JW5625
eco:b3699
PATRICifig|511145.12.peg.3823

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0419
EcoGeneiEG10424 gyrB

Phylogenomic databases

eggNOGiENOG4105C7D Bacteria
COG0187 LUCA
HOGENOMiHOG000075155
InParanoidiP0AES6
KOiK02470
PhylomeDBiP0AES6

Enzyme and pathway databases

BioCyciEcoCyc:EG10424-MONOMER
MetaCyc:EG10424-MONOMER
BRENDAi5.99.1.3 2026

Miscellaneous databases

EvolutionaryTraceiP0AES6

Protein Ontology

More...
PROi
PR:P0AES6

Family and domain databases

CDDicd00075 HATPase_c, 1 hit
cd03366 TOPRIM_TopoIIA_GyrB, 1 hit
Gene3Di3.30.230.10, 1 hit
3.30.565.10, 1 hit
3.40.50.670, 2 hits
HAMAPiMF_01898 GyrB, 1 hit
InterProiView protein in InterPro
IPR002288 DNA_gyrase_B_C
IPR011557 GyrB
IPR003594 HATPase_C
IPR036890 HATPase_C_sf
IPR020568 Ribosomal_S5_D2-typ_fold
IPR014721 Ribosomal_S5_D2-typ_fold_subgr
IPR001241 Topo_IIA
IPR013760 Topo_IIA-like_dom_sf
IPR013759 Topo_IIA_B_C
IPR013506 Topo_IIA_bsu_dom2
IPR018522 TopoIIA_CS
IPR006171 TOPRIM_domain
IPR034160 TOPRIM_GyrB
PANTHERiPTHR10169 PTHR10169, 1 hit
PfamiView protein in Pfam
PF00204 DNA_gyraseB, 1 hit
PF00986 DNA_gyraseB_C, 1 hit
PF02518 HATPase_c, 1 hit
PF01751 Toprim, 1 hit
SMARTiView protein in SMART
SM00387 HATPase_c, 1 hit
SM00433 TOP2c, 1 hit
SUPFAMiSSF54211 SSF54211, 1 hit
SSF55874 SSF55874, 1 hit
SSF56719 SSF56719, 1 hit
TIGRFAMsiTIGR01059 gyrB, 1 hit
PROSITEiView protein in PROSITE
PS00177 TOPOISOMERASE_II, 1 hit
PS50880 TOPRIM, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGYRB_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0AES6
Secondary accession number(s): O08438, P06982, Q2M811
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: December 5, 2018
This is version 130 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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