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Entry version 45 (13 Nov 2019)
Sequence version 1 (16 Apr 2014)
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Protein

DNA gyrase subunit A

Gene

gyrA

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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, while in the absence of ATP it relaxes supercoiled dsDNA (PubMed:15047530, PubMed:16377674, PubMed:16876125, PubMed:17015625, PubMed:18426901, PubMed:19060136, PubMed:22844097, PubMed:20805881). Also catalyzes the interconversion of other topological isomers of dsDNA rings, including catenanes (PubMed:16876125, PubMed:19060136, PubMed:22457352). Gyrase from M.tuberculosis has higher decatenation than supercoiling activity compared to E.coli; as M.tuberculosis only has 1 type II topoisomerase, gyrase has to fulfill the decatenation function of topoisomerase IV as well (PubMed:16876125, PubMed:22457352, PubMed:23869946). At comparable concentrations M.tuberculosis gyrase cannot introduce as many negative supercoils into DNA as the E.coli enzyme, and its ATPase activity is lower, perhaps because it does not couple DNA wrapping and ATP binding as well as E.coli (PubMed:22457352).10 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:15047530). In the presence of quinolones this intermediate can be trapped and is used as an indicator of drug toxicity (PubMed:16377674, PubMed:23869946). DNA gyrase is intrinsically more resistant to fluoroquinolone drugs than in E.coli, mutating it to resemble E.coli increases its susceptibility to fluoroquinolones (most quinolone-resistant mutations are in this subunit) (PubMed:18426901).3 Publications1 Publication
Gyrase from M.tuberculosis is usually assayed in the presence of potassium glutamate (KGlu); KGlu stimulates supercoiling but inhibits DNA relaxation activity, and has concentration-dependent effects on GyrA-box mutants (PubMed:16876125, PubMed:23869946).2 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 ‘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

Ca2+1 PublicationNote: May bind up to 2 Ca2+ per subunit, Ca2+ does not substitute for supercoiling activity, but is required for relaxation, probably by an interaction with this subunit (PubMed:22844097). This subunit has altered protease sensitivity in the presence of Ca2+, which might reflect regulation (PubMed:22844097).1 Publication

<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

DNA supercoiling inhibited by (fluoro)quinoline antibiotics such as sparfloxacin and levofloxacin, which usually act on GyrA (PubMed:15047530, PubMed:17015625). DNA supercoiling inhibited by the coumarin antibiotic novobiocin which acts on GyrB (PubMed:16876125). Quinolones lead to gyrase-mediated dsDNA cleavage while preventing reclosure (PubMed:15047530, PubMed:16876125, PubMed:23869946). DNA supercoiling activity inhibited by aminopyrazinamide and pyrrolamide derivatives, probably via effects on the GyrB subunit (PubMed:23268609, PubMed:24126580). DNA relaxation inhibited by ATP and its analogs (PubMed:16876125). DNA supercoiling, relaxation, decatenation and quinolone-promoted DNA cleavage are inhibited by MfpA (50% inhibition occurs at 2 µM), inhibition of gyrase activites is enhanced in a concentration-dependent manner by MfpA (PubMed:19060136).7 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 sitei129O-(5'-phospho-DNA)-tyrosine intermediateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) of the calcium-binding region(s) within the protein. One common calcium-binding motif is the EF-hand, but other calcium-binding motifs also exist.<p><a href='/help/ca_bind' target='_top'>More...</a></p>Calcium bindingi504 – 5161 PublicationAdd BLAST13

<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

<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, Calcium, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MTBH37RV:G185E-4117-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 annotation2 Publications)
Alternative name(s):
Type IIA topoisomerase subunit GyrA
<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
Ordered Locus Names:Rv0006
ORF Names:MTCY10H4.04
<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>OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
<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 identifieri83332 [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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
<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
  • UP000001584 <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

Organism-specific databases

Mycobacterium tuberculosis strain H37Rv genome database

More...
TubercuListi
Rv0006

<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>Mutagenesisi80T → A: Slight resistance to fluoroquinolones. Hypersusceptibile, 2-to 14-fold higher sensitivity to fluoroquinolones, 2- to 8-fold more efficient in fluoroquinolone-induced DNA cleavage; when associated with G-90. 1 Publication1
Mutagenesisi88G → A: Confers fluoroquinolone resistance, IC(50) is 2- to 26-fold higher than wild-type. 1 Publication1
Mutagenesisi88G → C: Confers fluoroquinolone resistance, IC(50) is 3- to 43-fold higher than wild-type, in strains H37Ra and H37Rv. 2 Publications1
Mutagenesisi90 – 94ASIYD → VSIYG: 80-fold increased resistance to fluoroquinolones, 32- to 64-fold reduction in fluoroquinolone-induced DNA cleavage. 1 Publication5
Mutagenesisi90A → G: 4- to 16-fold more efficient in fluoroquinolone-induced DNA cleavage alone. Hypersusceptibile, 2- to 14-fold higher sensitivity to fluoroquinolones, 2- to 8-fold more efficient in fluoroquinolone-induced DNA cleavage; when associated with A-80. 1 Publication1
Mutagenesisi90A → S: Increased susceptibility to fluoroquinolones (makes sequence more like E.coli), supercoiling, relaxation, decatenation activities still inhibited by MfpA. 2 Publications1
Mutagenesisi90A → V: 17-fold increased resistance to fluoroquinolones, 4- to 8-fold reduction in fluoroquinolone-induced DNA cleavage. 1 Publication1
Mutagenesisi94D → G or H: 25- 45-fold increased resistance to fluoroquinolones, 4- to 8-fold reduction in fluoroquinolone-induced DNA cleavage. Supercoiling, relaxation, decatenation activities no longer inhibited by MfpA. 2 Publications1
Mutagenesisi94D → H: Confers ofloxacin resistance. 1 Publication1
Mutagenesisi504 – 514DVSDEDLIARE → AVSDAALIARA: Significant reduction in DNA wrapping and supercoiling activity, no change in decatanation or relaxation activities. 1 PublicationAdd BLAST11
Mutagenesisi508 – 509ED → AA: Slight reduction in supercoiling activity. 1 Publication2
Mutagenesisi538K → R: Wild-type decatenase activity (changes residue to match E.coli). 1 Publication1
Mutagenesisi540 – 543GGKG → AAKA: No supercoiling activity, almost wild-type decatenation activity, wild-type fluoroquinolone-induced DNA cleavage. 1 Publication4
Mutagenesisi540G → A: No change in supercoiling activity, wild-type decatenation or fluoroquinolone-induced DNA cleavage. 1 Publication1
Mutagenesisi541G → A: Reduced supercoiling activity, wild-type decatenation and fluoroquinolone-induced DNA cleavage. 1 Publication1
Mutagenesisi543G → A: Reduced supercoiling activity, wild-type decatenation and fluoroquinolone-induced DNA cleavage. 1 Publication1
Mutagenesisi543G → K: No supercoiling activity, wild-type decatenation and fluoroquinolone-induced DNA cleavage. 1 Publication1
Mutagenesisi544 – 545VQ → KS: Wild-type decatenase activity (changes residues to match E.coli). 1 Publication2
Mutagenesisi746 – 749GGKG → AAKA: No supercoiling or decatenation activity, decreased fluoroquinolone-induced DNA cleavage. 1 Publication4
Mutagenesisi746G → A: Wild-type supercoiling, decatenation and fluoroquinolone-induced DNA cleavage. 1 Publication1
Mutagenesisi747G → A: Wild-type supercoiling, decatenation and fluoroquinolone-induced DNA cleavage. 1 Publication1
Mutagenesisi749G → A: No supercoiling or decatenation activity, decreased fluoroquinolone-induced DNA cleavage. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4165

DrugCentral

More...
DrugCentrali
P9WG47

<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 methionineiRemovedCombined sources
<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_00001452432 – 838DNA gyrase subunit AAdd BLAST837

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylthreonineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

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

More...
PaxDbi
P9WG47

PRoteomics IDEntifications database

More...
PRIDEi
P9WG47

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P9WG47

<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. In the heterotetramer, GyrA contains the active site tyrosine that forms a transient covalent intermediate with DNA, while GyrB binds cofactors and catalyzes ATP hydrolysis (PubMed:15047530).

UniRule annotation1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
83332.Rv0006

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P9WG47

<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

1838
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

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SMRi
P9WG47

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

<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>Domaini504 – 516EF-hand1 PublicationAdd BLAST13

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>Regioni514 – 838C-terminal domain CTD2 PublicationsAdd BLAST325

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>Motifi537 – 543GyrA-box1 PublicationUniRule annotation7
Motifi743 – 749GyrA-box-11 Publication7

<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

The N-terminal domain (residues 1-502, also called GA57BK) forms a dimer; when reconstituted with intact GyrB or the C-terminus of GyrB (residues 448-675) can catalyze quinolone-mediated DNA breaks (PubMed:20805881). The C-terminal domain (CTD, residues 514-838) contains 6 tandemly repeated subdomains known as blades, each of which is composed of a 4-stranded antiparallel beta-sheet (PubMed:22457352, PubMed:23869946). The blades form a circular-shaped beta-pinwheel fold arranged in a spiral around a screw axis, which binds DNA (PubMed:22457352, PubMed:23869946). Unlike in E.coli, isolated CTD both binds and wraps DNA and is able to introduce writhe into DNA, but the holoenzyme in M.tuberculosis is missing the GyrA acidic tail found in E.coli and thus does not couple DNA wrapping and ATP binding as well as E.coli (PubMed:22457352). There are 2 GyrA-boxes in the CTD; mutations in GyrA-box (residues 537-543, the canonical box) affect supercoiling but not decatenation, those in GyrA-box-1 (residues 743-749, conserved in some Actinobacteria) affect both, suggesting there is a novel DNA-binding pathway in M.tuberculosis compared to E.coli (PubMed:23869946).3 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

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eggNOGi
ENOG4105C24 Bacteria
COG0188 LUCA

KEGG Orthology (KO)

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KOi
K02469

Database for complete collections of gene phylogenies

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PhylomeDBi
P9WG47

Family and domain databases

Conserved Domains Database

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CDDi
cd00187 TOP4c, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.268.10, 1 hit
2.120.10.90, 1 hit
3.90.199.10, 1 hit

HAMAP database of protein families

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HAMAPi
MF_01897 GyrA, 1 hit

Integrated resource of protein families, domains and functional sites

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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

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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

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SMARTi
View protein in SMART
SM00434 TOP4c, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF101904 SSF101904, 1 hit
SSF56719 SSF56719, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00018 EF_HAND_1, 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.

P9WG47-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTDTTLPPDD SLDRIEPVDI EQEMQRSYID YAMSVIVGRA LPEVRDGLKP
60 70 80 90 100
VHRRVLYAMF DSGFRPDRSH AKSARSVAET MGNYHPHGDA SIYDSLVRMA
110 120 130 140 150
QPWSLRYPLV DGQGNFGSPG NDPPAAMRYT EARLTPLAME MLREIDEETV
160 170 180 190 200
DFIPNYDGRV QEPTVLPSRF PNLLANGSGG IAVGMATNIP PHNLRELADA
210 220 230 240 250
VFWALENHDA DEEETLAAVM GRVKGPDFPT AGLIVGSQGT ADAYKTGRGS
260 270 280 290 300
IRMRGVVEVE EDSRGRTSLV ITELPYQVNH DNFITSIAEQ VRDGKLAGIS
310 320 330 340 350
NIEDQSSDRV GLRIVIEIKR DAVAKVVINN LYKHTQLQTS FGANMLAIVD
360 370 380 390 400
GVPRTLRLDQ LIRYYVDHQL DVIVRRTTYR LRKANERAHI LRGLVKALDA
410 420 430 440 450
LDEVIALIRA SETVDIARAG LIELLDIDEI QAQAILDMQL RRLAALERQR
460 470 480 490 500
IIDDLAKIEA EIADLEDILA KPERQRGIVR DELAEIVDRH GDDRRTRIIA
510 520 530 540 550
ADGDVSDEDL IAREDVVVTI TETGYAKRTK TDLYRSQKRG GKGVQGAGLK
560 570 580 590 600
QDDIVAHFFV CSTHDLILFF TTQGRVYRAK AYDLPEASRT ARGQHVANLL
610 620 630 640 650
AFQPEERIAQ VIQIRGYTDA PYLVLATRNG LVKKSKLTDF DSNRSGGIVA
660 670 680 690 700
VNLRDNDELV GAVLCSAGDD LLLVSANGQS IRFSATDEAL RPMGRATSGV
710 720 730 740 750
QGMRFNIDDR LLSLNVVREG TYLLVATSGG YAKRTAIEEY PVQGRGGKGV
760 770 780 790 800
LTVMYDRRRG RLVGALIVDD DSELYAVTSG GGVIRTAARQ VRKAGRQTKG
810 820 830
VRLMNLGEGD TLLAIARNAE ESGDDNAVDA NGADQTGN
Length:838
Mass (Da):92,274
Last modified:April 16, 2014 - 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:i84DAFE13D74D76D7
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 conflicti83N → K in AAC36878 (PubMed:8294019).Curated1
Sequence conflicti712L → V in AAA83017 (PubMed:8031045).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 varianti90A → V Confers ciprofloxacin resistance, in clinical isolate. 1 Publication1
Natural varianti91S → P Confers ciprofloxacin resistance, in clinical isolate. 1 Publication1
Natural varianti94D → A Confers ciprofloxacin resistance, in clinical isolate. 1 Publication1
Natural varianti94D → G Confers ciprofloxacin resistance, in clinical isolate. 1 Publication1
Natural varianti94D → H Confers ciprofloxacin resistance, in clinical isolate. 1 Publication1
Natural varianti94D → N Confers ciprofloxacin resistance, in clinical isolate. 1 Publication1
Natural varianti94D → Y Confers ciprofloxacin resistance, in clinical isolate. 1 Publication1

Sequence databases

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EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
L27512 Genomic DNA Translation: AAA83017.1
JX303241 Genomic DNA Translation: AFR90330.1
AL123456 Genomic DNA Translation: CCP42728.1
L11919 Unassigned DNA Translation: AAC36878.1
X72872 Genomic DNA Translation: CAA51386.1

Protein sequence database of the Protein Information Resource

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PIRi
D70698

NCBI Reference Sequences

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RefSeqi
NP_214520.1, NC_000962.3
WP_003917265.1, NZ_NVQJ01000005.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

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EnsemblBacteriai
CCP42728; CCP42728; Rv0006

Database of genes from NCBI RefSeq genomes

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GeneIDi
887105

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mtu:Rv0006
mtv:RVBD_0006

<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
L27512 Genomic DNA Translation: AAA83017.1
JX303241 Genomic DNA Translation: AFR90330.1
AL123456 Genomic DNA Translation: CCP42728.1
L11919 Unassigned DNA Translation: AAC36878.1
X72872 Genomic DNA Translation: CAA51386.1
PIRiD70698
RefSeqiNP_214520.1, NC_000962.3
WP_003917265.1, NZ_NVQJ01000005.1

3D structure databases

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Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3IFZX-ray2.70A/B1-501[»]
3ILWX-ray1.60A/B34-500[»]
3UC1X-ray1.65A514-838[»]
4G3NX-ray1.40A512-838[»]
5BS8X-ray2.40A/C2-500[»]
5BTAX-ray2.55A/C2-500[»]
5BTCX-ray2.55A/C2-500[»]
5BTDX-ray2.50A/C2-500[»]
5BTFX-ray2.61A/C2-500[»]
5BTGX-ray2.50A/C2-500[»]
5BTIX-ray2.50A/C2-500[»]
5BTLX-ray2.50A/C2-500[»]
5BTNX-ray2.50A/C2-500[»]
6GAUX-ray3.30A/B2-501[»]
6GAVX-ray2.60A/B2-501[»]
SMRiP9WG47
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv0006

Chemistry databases

BindingDBiP9WG47
ChEMBLiCHEMBL4165
DrugCentraliP9WG47

PTM databases

iPTMnetiP9WG47

Proteomic databases

PaxDbiP9WG47
PRIDEiP9WG47

Genome annotation databases

EnsemblBacteriaiCCP42728; CCP42728; Rv0006
GeneIDi887105
KEGGimtu:Rv0006
mtv:RVBD_0006

Organism-specific databases

TubercuListiRv0006

Phylogenomic databases

eggNOGiENOG4105C24 Bacteria
COG0188 LUCA
KOiK02469
PhylomeDBiP9WG47

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-4117-MONOMER

Miscellaneous databases

Protein Ontology

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PROi
PR:P9WG47

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
PROSITEiView protein in PROSITE
PS00018 EF_HAND_1, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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_MYCTU
<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: P9WG47
Secondary accession number(s): J9VB15
, P71574, P97136, Q07702
<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 16, 2014
Last sequence update: April 16, 2014
Last modified: November 13, 2019
This is version 45 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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