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UniProtKB - P0AES4 (GYRA_ECOLI)

Entry version 137 (31 Jul 2019)
Sequence version 1 (20 Dec 2005)
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Protein

DNA gyrase subunit A

Gene

gyrA

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

A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to maintain chromosomes in an underwound state (PubMed:3031051, PubMed:186775, PubMed:7811004, PubMed:9148951, PubMed:12051842, PubMed:18642932, PubMed:19060136, PubMed:20356737, PubMed:22457353, PubMed:23294697, PubMed:19965760). This makes better substrates for topoisomerase IV (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 dsDNA rings, including catenanes (PubMed:22457352). Relaxes negatively supercoiled DNA in an ATP-independent manner (PubMed:337300). E.coli gyrase has higher supercoiling activity than many other 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).17 Publications
Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.

Miscellaneous

When the enzyme transiently cleaves DNA a phosphotyrosine bond is formed between GyrA and DNA (PubMed:3031051). In the presence of quinolones this intermediate can be trapped and is used as an indicator of drug toxicity (PubMed:12051842). The enzyme-DNA intermediate is also the target of a number of topoisomerase poisons, including toxin CcdB (PubMed:1324324, PubMed:8254658).1 Publication3 Publications
Few gyrases are as efficient as E.coli at forming negative supercoils (PubMed:22457352, PubMed:17400739). Not all organisms have 2 type II topoisomerases; in organisms with a single type II topoisomerase this enzyme also has to decatenate newly replicated chromosomes.UniRule annotation2 Publications

<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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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. 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). 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). Pyrrolopyrimidines inhibit both GyrB and its paralog in topoisomerase IV (parE) (PubMed:23294697). Pyrazolthiazoles also inhibit the ATPase activity of GyrB (PubMed:20356737). DNA supercoiling and relaxation are both inhibited by oxolinic acid (PubMed:337300). Acriflavine inhibits supercoiling activity 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).6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei122O-(5'-phospho-DNA)-tyrosine intermediateUniRule annotation1 Publication1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG10423-MONOMER
ECOL316407:JW2225-MONOMER
MetaCyc:EG10423-MONOMER

<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 AUniRule annotation (EC:5.6.2.2UniRule annotation5 Publications)
<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:gyrAUniRule annotation
Synonyms:hisW, nalA1 Publication, parD
Ordered Locus Names:b2231, JW2225
<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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<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		EG10423 gyrA

<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

Complete GO annotation on QuickGO ...

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>Mutagenesisi32R → A or Q: Nearly abolishes DNA supercoiling. Reduces quinolone-induced DNA cleavage and relaxation. 1 Publication1
Mutagenesisi47R → Q: Nearly abolishes DNA supercoiling. Reduces quinolone-induced DNA cleavage. Slightly reduces DNA relaxation. 1 Publication1
Mutagenesisi78H → A: Nearly abolishes DNA supercoiling. Reduces quinolone-induced DNA cleavage and DNA relaxation. 1 Publication1
Mutagenesisi80H → A: Reduces DNA supercoiling. Slightly reduces quinolone-induced DNA cleavage. No effect on DNA relaxation. 1 Publication1
Mutagenesisi83S → A: Resistant to fluoroquinolones. 1 Publication1
Mutagenesisi106Q → R: Resistant to fluoroquinolones. 1 Publication1
Mutagenesisi462R → C in gyrA462; resistant to cytotoxic protein CcdB, but not to the quinoline antibiotic enoxacin, has no effect on DNA supercoiling. Does not interact with CcdB. 2 Publications1
Mutagenesisi560 – 566QRRGGKG → AAAAAAA: Loss of gyrase-mediated DNA wrapping, nearly complete loss of DNA supercoiling activity, no change in DNA supercoil relaxation or DNA decatenation activity. 1 Publication7
Mutagenesisi560 – 566Missing : Loss of gyrase-mediated DNA wrapping, nearly complete loss of DNA supercoiling activity, no change in DNA supercoil relaxation or DNA decatenation activity. 1 Publication7
Mutagenesisi842 – 856Missing : Gains ability to wrap DNA around itself in the absence of GyrB; holoenzyme gains ability to wrap DNA in the absence of ATP analogs, but reduces ATP-dependent supercoiling activity 50-fold, DNA is not as extensively negatively supercoiled, has 10-fold less ATP-independent negative supercoiled DNA relaxation activity, no change in ATPase activity of holoenzyme, no change in decatenation ability. Isolated CTD gains ability to wrap DNA around itself in the absence of GyrB, binds DNA better than wild-type CTD. 2 PublicationsAdd BLAST15
Mutagenesisi854 – 875Missing : Isolated CTD gains ability to wrap DNA around itself in the absence of GyrB, binds DNA better than wild-type CTD. 1 PublicationAdd BLAST22

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1858

Drug and drug target database

More...DrugBanki		DB00537 Ciprofloxacin

<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_00001452322 – 875DNA gyrase subunit AAdd BLAST874

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P0AES4

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0AES4

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

More...PaxDbi		P0AES4

PRoteomics IDEntifications database

More...PRIDEi		P0AES4

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P0AES4

<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:12051842, PubMed:18642932, PubMed:19965760, PubMed:9148951). Can form a 2:2 complex with toxin CcdB in which GyrA is inactive; rejuvenation of GyrA2CcdB2 is effected by CcdA (PubMed:15854646, PubMed:1324324, PubMed:8254658, PubMed:8604132).

8 Publications

<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

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4262132, 294 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-2177 GyrA-GyrB complex

Database of interacting proteins

More...DIPi		DIP-36179N

Protein interaction database and analysis system

More...IntActi		P0AES4, 53 interactors

Molecular INTeraction database

More...MINTi		P0AES4

STRING: functional protein association networks

More...STRINGi		511145.b2231

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P0AES4

<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

1875
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P0AES4

Database of comparative protein structure models

More...ModBasei		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P0AES4

<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

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>Regioni531 – 841C-terminal domain (CTD)1 PublicationAdd BLAST311
Regioni842 – 875Acidic tail1 PublicationAdd BLAST34

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi560 – 566GyrA-box1 PublicationUniRule annotation7

<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

An N-terminal fragment (residues 1-523) can be reconstituted with GyrB, but the complex no longer has negative supercoiling or ATP-independent DNA relaxation activities, although it is capable of DNA cleavage; ATP-dependent relaxation is inhibited by novobiocin and non-hydrolyzable ATP analogs (PubMed:8962066). The fragment has ATP-dependent DNA relaxation and 30-fold improved decatenation activities, unlike holoenzyme it preferentially binds supercoiled DNA (PubMed:8962066). This N-terminal fragment becomes a topoisomerase IV-like enzyme; it poorly complements a temperature-sensitive parC mutation (parC is the topoisomerase IV paralog of gyrA) (PubMed:8962066).1 Publication
The C-terminal domain (CTD, approximately residues 535-841) contains 6 tandemly repeated subdomains known as blades, each of which is composed of a 4-stranded antiparallel beta-sheet (PubMed:15897198). The blades form a circular-shaped beta-pinwheel fold arranged in a spiral around a screw axis, to which DNA probably binds, inducing strong positive superhelicity (about 0.8 links/protein) (PubMed:15897198). The non-conserved, C-terminal acidic tail (residues 842-875) regulates wrapping and DNA-binding by the CTD; deletions within the tail show it is autoinhibitory for DNA wrapping and binding, and couples ATP hydrolysis to DNA strand passage (PubMed:22457353). The GyrA-box is a 7 amino acid motif found in the first blade of the CTD which is discriminative for gyrase versus topoisomerase IV activity (PubMed:9426128). The GyrA-box is required for wrapping of DNA around gyrase, and thus is essential for the DNA supercoiling activity but not DNA relaxation or decatenation activities of gyrase (PubMed:16332690).1 Publication3 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 GyrA/ParC subunit family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4105C24 Bacteria
COG0188 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000076278

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0AES4

KEGG Orthology (KO)

More...KOi		K02469

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0AES4

Family and domain databases

Conserved Domains Database

More...CDDi		cd00187 TOP4c, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.268.10, 1 hit
2.120.10.90, 1 hit
3.90.199.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_01897 GyrA, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR005743 GyrA
IPR006691 GyrA/parC_rep
IPR035516 Gyrase/topoIV_suA_C
IPR013760 Topo_IIA-like_dom_sf
IPR002205 Topo_IIA_A/C
IPR013758 Topo_IIA_A/C_ab
IPR013757 Topo_IIA_A_a_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF03989 DNA_gyraseA_C, 6 hits
PF00521 DNA_topoisoIV, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00434 TOP4c, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF101904 SSF101904, 1 hit
SSF56719 SSF56719, 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>. The information is filed in different subsections. The current subsections and their content are listed below:<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.

P0AES4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSDLAREITP VNIEEELKSS YLDYAMSVIV GRALPDVRDG LKPVHRRVLY 
        60         70         80         90        100
AMNVLGNDWN KAYKKSARVV GDVIGKYHPH GDSAVYDTIV RMAQPFSLRY 
       110        120        130        140        150
MLVDGQGNFG SIDGDSAAAM RYTEIRLAKI AHELMADLEK ETVDFVDNYD 
       160        170        180        190        200
GTEKIPDVMP TKIPNLLVNG SSGIAVGMAT NIPPHNLTEV INGCLAYIDD 
       210        220        230        240        250
EDISIEGLME HIPGPDFPTA AIINGRRGIE EAYRTGRGKV YIRARAEVEV 
       260        270        280        290        300
DAKTGRETII VHEIPYQVNK ARLIEKIAEL VKEKRVEGIS ALRDESDKDG 
       310        320        330        340        350
MRIVIEVKRD AVGEVVLNNL YSQTQLQVSF GINMVALHHG QPKIMNLKDI 
       360        370        380        390        400
IAAFVRHRRE VVTRRTIFEL RKARDRAHIL EALAVALANI DPIIELIRHA 
       410        420        430        440        450
PTPAEAKTAL VANPWQLGNV AAMLERAGDD AARPEWLEPE FGVRDGLYYL 
       460        470        480        490        500
TEQQAQAILD LRLQKLTGLE HEKLLDEYKE LLDQIAELLR ILGSADRLME 
       510        520        530        540        550
VIREELELVR EQFGDKRRTE ITANSADINL EDLITQEDVV VTLSHQGYVK 
       560        570        580        590        600
YQPLSEYEAQ RRGGKGKSAA RIKEEDFIDR LLVANTHDHI LCFSSRGRVY 
       610        620        630        640        650
SMKVYQLPEA TRGARGRPIV NLLPLEQDER ITAILPVTEF EEGVKVFMAT 
       660        670        680        690        700
ANGTVKKTVL TEFNRLRTAG KVAIKLVDGD ELIGVDLTSG EDEVMLFSAE 
       710        720        730        740        750
GKVVRFKESS VRAMGCNTTG VRGIRLGEGD KVVSLIVPRG DGAILTATQN 
       760        770        780        790        800
GYGKRTAVAE YPTKSRATKG VISIKVTERN GLVVGAVQVD DCDQIMMITD 
       810        820        830        840        850
AGTLVRTRVS EISIVGRNTQ GVILIRTAED ENVVGLQRVA EPVDEEDLDT 
       860        870 
IDGSAAEGDD EIAPEVDVDD EPEEE
Length:875
Mass (Da):96,964
Last modified:December 20, 2005 - v1
<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:i3FD5BD52A5969069
GO

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 varianti67A → S in PPA-10; quinolone-resistant. 1 Publication1
Natural varianti81G → C in NAL-97; quinolone-resistant. 1 Publication1
Natural varianti83S → L in NAL-51, NAL-112, NAL-118, NAL-119 and strains 58, 158, 218, 231 and 235; quinolone-resistant. 2 Publications1
Natural varianti83S → W in PPA-18 and strains 233 and 227; quinolone-resistant. 3 Publications1
Natural varianti84A → P in PPA-05; quinolone-resistant. 1 Publication1
Natural varianti87D → N in NAL-113 and OV6; quinolone-resistant. 2 Publications1
Natural varianti87D → V in strain: 202; partially quinolone-resistant. 1 Publication1
Natural varianti106Q → H in NAL-89; quinolone-resistant. 1 Publication1
Natural varianti678D → E in strain: 227. 1 Publication1
Natural varianti798I → IMMI in strain OV6; quinolone-resistant. 1 Publication1
Natural varianti828A → S in strain: 227. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
X06373 Genomic DNA Translation: CAA29676.1
X06744 Genomic DNA Translation: CAA29919.1
M15631 Genomic DNA Translation: AAA23948.1
U00096 Genomic DNA Translation: AAC75291.1
AP009048 Genomic DNA Translation: BAA16048.1
Y00544 Genomic DNA Translation: CAA68611.1

Protein sequence database of the Protein Information Resource

More...PIRi		S02340 ITECAP

NCBI Reference Sequences

More...RefSeqi		NP_416734.1, NC_000913.3
WP_001281242.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC75291; AAC75291; b2231
BAA16048; BAA16048; BAA16048

Database of genes from NCBI RefSeq genomes

More...GeneIDi		946614

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW2225
eco:b2231

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.4

<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
X06373 Genomic DNA Translation: CAA29676.1
X06744 Genomic DNA Translation: CAA29919.1
M15631 Genomic DNA Translation: AAA23948.1
U00096 Genomic DNA Translation: AAC75291.1
AP009048 Genomic DNA Translation: BAA16048.1
Y00544 Genomic DNA Translation: CAA68611.1
PIRiS02340 ITECAP
RefSeqiNP_416734.1, NC_000913.3
WP_001281242.1, NZ_LN832404.1

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
1AB4X-ray2.80A30-522[»]
1X75X-ray2.80A/B363-494[»]
1ZI0X-ray2.60A/B535-841[»]
2Y3PX-ray2.62A/B2-523[»]
3NUHX-ray3.10A1-525[»]
4ELYX-ray1.93A/B363-497[»]
SMRiP0AES4
ModBaseiSearch...

Protein-protein interaction databases

BioGridi4262132, 294 interactors
ComplexPortaliCPX-2177 GyrA-GyrB complex
DIPiDIP-36179N
IntActiP0AES4, 53 interactors
MINTiP0AES4
STRINGi511145.b2231

Chemistry databases

BindingDBiP0AES4
ChEMBLiCHEMBL1858
DrugBankiDB00537 Ciprofloxacin

2D gel databases

SWISS-2DPAGEiP0AES4

Proteomic databases

EPDiP0AES4
jPOSTiP0AES4
PaxDbiP0AES4
PRIDEiP0AES4

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75291; AAC75291; b2231
BAA16048; BAA16048; BAA16048
GeneIDi946614
KEGGiecj:JW2225
eco:b2231
PATRICifig|1411691.4.peg.4

Organism-specific databases

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

More...EchoBASEi		EB0418
EcoGeneiEG10423 gyrA

Phylogenomic databases

eggNOGiENOG4105C24 Bacteria
COG0188 LUCA
HOGENOMiHOG000076278
InParanoidiP0AES4
KOiK02469
PhylomeDBiP0AES4

Enzyme and pathway databases

BioCyciEcoCyc:EG10423-MONOMER
ECOL316407:JW2225-MONOMER
MetaCyc:EG10423-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0AES4

Protein Ontology

More...PROi		PR:P0AES4

Family and domain databases

CDDicd00187 TOP4c, 1 hit
Gene3Di1.10.268.10, 1 hit
2.120.10.90, 1 hit
3.90.199.10, 1 hit
HAMAPiMF_01897 GyrA, 1 hit
InterProiView protein in InterPro
IPR005743 GyrA
IPR006691 GyrA/parC_rep
IPR035516 Gyrase/topoIV_suA_C
IPR013760 Topo_IIA-like_dom_sf
IPR002205 Topo_IIA_A/C
IPR013758 Topo_IIA_A/C_ab
IPR013757 Topo_IIA_A_a_sf
PfamiView protein in Pfam
PF03989 DNA_gyraseA_C, 6 hits
PF00521 DNA_topoisoIV, 1 hit
SMARTiView protein in SMART
SM00434 TOP4c, 1 hit
SUPFAMiSSF101904 SSF101904, 1 hit
SSF56719 SSF56719, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiGYRA_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: P0AES4
Secondary accession number(s): P09097
<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: December 20, 2005
Last sequence update: December 20, 2005
Last modified: July 31, 2019
This is version 137 of the entry and version 1 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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