Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

DNA gyrase subunit A (EC 5.99.1.3) (Type IIA topoisomerase subunit GyrA)

 GYRA_MYCTU              Reviewed;         838 AA.
P9WG47; J9VB15; P71574; P97136; Q07702;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
12-SEP-2018, entry version 35.
RecName: Full=DNA gyrase subunit A {ECO:0000255|HAMAP-Rule:MF_01897};
EC=5.99.1.3 {ECO:0000255|HAMAP-Rule:MF_01897, ECO:0000269|PubMed:15047530, ECO:0000269|PubMed:16876125};
AltName: Full=Type IIA topoisomerase subunit GyrA;
Name=gyrA {ECO:0000255|HAMAP-Rule:MF_01897}; OrderedLocusNames=Rv0006;
ORFNames=MTCY10H4.04;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-90; PRO-91; ALA-94;
GLY-94; HIS-94; ASN-94 AND TYR-94, MUTAGENESIS OF GLY-88, AND
ANTIBIOTIC RESISTANCE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=8031045; DOI=10.1128/AAC.38.4.773;
Takiff H.E., Salazar L., Guerrero C., Philipp W., Huang W.M.,
Kreiswirth B., Cole S.T., Jacobs W.R. Jr., Telenti A.;
"Cloning and nucleotide sequence of Mycobacterium tuberculosis gyrA
and gyrB genes and detection of quinolone resistance mutations.";
Antimicrob. Agents Chemother. 38:773-780(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=2997164;
PubMed=22972833; DOI=10.1128/JCM.01893-12;
Daum L.T., Rodriguez J.D., Worthy S.A., Ismail N.A., Omar S.V.,
Dreyer A.W., Fourie P.B., Hoosen A.A., Chambers J.P., Fischer G.W.;
"Next-generation ion torrent sequencing of drug resistance mutations
in Mycobacterium tuberculosis strains.";
J. Clin. Microbiol. 50:3831-3837(2012).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 82-188.
STRAIN=ATCC 25618 / H37Rv;
PubMed=8294019; DOI=10.1016/0378-1119(93)90481-H;
Mizrahi V., Huberts P., Dawes S.S., Dudding L.R.;
"A PCR method for the sequence analysis of the gyrA, polA and rnhA
gene segments from mycobacteria.";
Gene 136:287-290(1993).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 89-124, MUTAGENESIS OF ASP-94,
AND ANTIBIOTIC RESISTANCE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=8035042; DOI=10.1093/infdis/170.2.479;
Cambau E., Sougakoff W., Besson M., Truffot-Pernot C., Grosset J.,
Jarlier V.;
"Selection of a gyrA mutant of Mycobacterium tuberculosis resistant to
fluoroquinolones during treatment with ofloxacin.";
J. Infect. Dis. 170:479-483(1994).
[6]
FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND
REACTION MECHANISM.
STRAIN=ATCC 25618 / H37Rv;
PubMed=15047530; DOI=10.1128/AAC.48.4.1281-1288.2004;
Aubry A., Pan X.S., Fisher L.M., Jarlier V., Cambau E.;
"Mycobacterium tuberculosis DNA gyrase: interaction with quinolones
and correlation with antimycobacterial drug activity.";
Antimicrob. Agents Chemother. 48:1281-1288(2004).
[7]
FUNCTION, MUTAGENESIS OF THR-80; ALA-90 AND ASP-94, AND ANTIBIOTIC
RESISTANCE.
STRAIN=H37Rv;
PubMed=16377674; DOI=10.1128/AAC.50.1.104-112.2006;
Aubry A., Veziris N., Cambau E., Truffot-Pernot C., Jarlier V.,
Fisher L.M.;
"Novel gyrase mutations in quinolone-resistant and -hypersusceptible
clinical isolates of Mycobacterium tuberculosis: functional analysis
of mutant enzymes.";
Antimicrob. Agents Chemother. 50:104-112(2006).
[8]
FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
STRAIN=H37Rv;
PubMed=16876125; DOI=10.1016/j.bbrc.2006.07.017;
Aubry A., Fisher L.M., Jarlier V., Cambau E.;
"First functional characterization of a singly expressed bacterial
type II topoisomerase: the enzyme from Mycobacterium tuberculosis.";
Biochem. Biophys. Res. Commun. 348:158-165(2006).
[9]
FUNCTION, ACTIVITY REGULATION, MUTAGENESIS OF GLY-88, AND
ANTIBIOTIC-RESISTANCE.
STRAIN=H37Rv;
PubMed=17015625; DOI=10.1128/AAC.00944-06;
Matrat S., Veziris N., Mayer C., Jarlier V., Truffot-Pernot C.,
Camuset J., Bouvet E., Cambau E., Aubry A.;
"Functional analysis of DNA gyrase mutant enzymes carrying mutations
at position 88 in the A subunit found in clinical strains of
Mycobacterium tuberculosis resistant to fluoroquinolones.";
Antimicrob. Agents Chemother. 50:4170-4173(2006).
[10]
FUNCTION, MUTAGENESIS OF ALA-90, AND ANTIBIOTIC SUSCEPTIBILITY.
PubMed=18426901; DOI=10.1128/AAC.01380-07;
Matrat S., Aubry A., Mayer C., Jarlier V., Cambau E.;
"Mutagenesis in the alpha3alpha4 GyrA helix and in the Toprim domain
of GyrB refines the contribution of Mycobacterium tuberculosis DNA
gyrase to intrinsic resistance to quinolones.";
Antimicrob. Agents Chemother. 52:2909-2914(2008).
[11]
FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF ALA-90 AND ASP-94.
STRAIN=H37Rv;
PubMed=19060136; DOI=10.1128/JB.01205-08;
Merens A., Matrat S., Aubry A., Lascols C., Jarlier V., Soussy C.J.,
Cavallo J.D., Cambau E.;
"The pentapeptide repeat proteins MfpAMt and QnrB4 exhibit opposite
effects on DNA gyrase catalytic reactions and on the ternary gyrase-
DNA-quinolone complex.";
J. Bacteriol. 191:1587-1594(2009).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[13]
FUNCTION, POSSIBLE CALCIUM COFACTOR, POSSIBLE EF-HAND DOMAIN, AND
MUTAGENESIS OF 504-ASP--ASP-514 AND 508-GLU-ASP-509.
PubMed=22844097; DOI=10.1093/nar/gks704;
Karkare S., Yousafzai F., Mitchenall L.A., Maxwell A.;
"The role of Ca(2+) in the activity of Mycobacterium tuberculosis DNA
gyrase.";
Nucleic Acids Res. 40:9774-9787(2012).
[14]
ACTIVITY REGULATION.
STRAIN=H37Rv;
PubMed=23268609; DOI=10.1021/cb300510w;
Shirude P.S., Madhavapeddi P., Tucker J.A., Murugan K., Patil V.,
Basavarajappa H., Raichurkar A.V., Humnabadkar V., Hussein S.,
Sharma S., Ramya V.K., Narayan C.B., Balganesh T.S.,
Sambandamurthy V.K.;
"Aminopyrazinamides: novel and specific GyrB inhibitors that kill
replicating and nonreplicating Mycobacterium tuberculosis.";
ACS Chem. Biol. 8:519-523(2013).
[15]
ACTIVITY REGULATION.
STRAIN=ATCC 27294 / TMC 102 / H37Rv;
PubMed=24126580; DOI=10.1128/AAC.01751-13;
P S.H., Solapure S., Mukherjee K., Nandi V., Waterson D., Shandil R.,
Balganesh M., Sambandamurthy V.K., Raichurkar A.K., Deshpande A.,
Ghosh A., Awasthy D., Shanbhag G., Sheikh G., McMiken H., Puttur J.,
Reddy J., Werngren J., Read J., Kumar M., R M., Chinnapattu M.,
Madhavapeddi P., Manjrekar P., Basu R., Gaonkar S., Sharma S.,
Hoffner S., Humnabadkar V., Subbulakshmi V., Panduga V.;
"Optimization of pyrrolamides as mycobacterial GyrB ATPase inhibitors:
structure-activity relationship and in vivo efficacy in a mouse model
of tuberculosis.";
Antimicrob. Agents Chemother. 58:61-70(2014).
[16]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 34-500.
PubMed=19787774; DOI=10.1002/prot.22600;
Tretter E.M., Schoeffler A.J., Weisfield S.R., Berger J.M.;
"Crystal structure of the DNA gyrase GyrA N-terminal domain from
Mycobacterium tuberculosis.";
Proteins 78:492-495(2010).
[17]
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-501, FUNCTION, AND DOMAIN.
PubMed=20805881; DOI=10.1371/journal.pone.0012245;
Piton J., Petrella S., Delarue M., Andre-Leroux G., Jarlier V.,
Aubry A., Mayer C.;
"Structural insights into the quinolone resistance mechanism of
Mycobacterium tuberculosis DNA gyrase.";
PLoS ONE 5:E12245-E12245(2010).
[18]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 514-838, FUNCTION, DOMAIN,
AND DNA-BINDING.
STRAIN=ATCC 25618 / H37Rv;
PubMed=22457352; DOI=10.1074/jbc.M112.345736;
Tretter E.M., Berger J.M.;
"Mechanisms for defining supercoiling set point of DNA gyrase
orthologs: II. The shape of the GyrA subunit C-terminal domain (CTD)
is not a sole determinant for controlling supercoiling efficiency.";
J. Biol. Chem. 287:18645-18654(2012).
[19]
X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 512-838, FUNCTION, DOMAIN,
DNA-BINDING, AND MUTAGENESIS OF LYS-538; 540-GLY--GLY-543; GLY-540;
GLY-541; GLY-543; 544-VAL-GLN-545; 746-GLY--GLY-749; GLY-747; GLY-749
AND GLY-749.
STRAIN=H37Rv;
PubMed=23869946; DOI=10.1042/BJ20130430;
Bouige A., Darmon A., Piton J., Roue M., Petrella S., Capton E.,
Forterre P., Aubry A., Mayer C.;
"Mycobacterium tuberculosis DNA gyrase possesses two functional GyrA-
boxes.";
Biochem. J. 455:285-294(2013).
-!- FUNCTION: 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). {ECO:0000269|PubMed:15047530,
ECO:0000269|PubMed:16377674, ECO:0000269|PubMed:16876125,
ECO:0000269|PubMed:17015625, ECO:0000269|PubMed:18426901,
ECO:0000269|PubMed:19060136, ECO:0000269|PubMed:20805881,
ECO:0000269|PubMed:22457352, ECO:0000269|PubMed:22844097,
ECO:0000269|PubMed:23869946}.
-!- FUNCTION: 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.
-!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining
of double-stranded DNA. {ECO:0000255|HAMAP-Rule:MF_01897,
ECO:0000269|PubMed:15047530, ECO:0000269|PubMed:16876125}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:22844097};
Note=May bind up to 2 Ca(2+) per subunit, Ca(2+) 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 Ca(2+), which might reflect regulation
(PubMed:22844097). {ECO:0000269|PubMed:22844097};
-!- ACTIVITY REGULATION: 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 uM), inhibition of
gyrase activites is enhanced in a concentration-dependent manner
by MfpA (PubMed:19060136). {ECO:0000269|PubMed:15047530,
ECO:0000269|PubMed:16876125, ECO:0000269|PubMed:17015625,
ECO:0000269|PubMed:19060136, ECO:0000269|PubMed:23268609,
ECO:0000269|PubMed:23869946, ECO:0000269|PubMed:24126580}.
-!- SUBUNIT: 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).
{ECO:0000255|HAMAP-Rule:MF_01897, ECO:0000269|PubMed:15047530}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01897}.
-!- DOMAIN: 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). {ECO:0000269|PubMed:20805881,
ECO:0000269|PubMed:22457352, ECO:0000269|PubMed:23869946}.
-!- 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). {ECO:0000269|PubMed:18426901,
ECO:0000305|PubMed:15047530, ECO:0000305|PubMed:16377674,
ECO:0000305|PubMed:23869946}.
-!- MISCELLANEOUS: 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). {ECO:0000269|PubMed:16876125,
ECO:0000269|PubMed:23869946}.
-!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
family. {ECO:0000255|HAMAP-Rule:MF_01897}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; L27512; AAA83017.1; -; Genomic_DNA.
EMBL; JX303241; AFR90330.1; -; Genomic_DNA.
EMBL; AL123456; CCP42728.1; -; Genomic_DNA.
EMBL; L11919; AAC36878.1; -; Unassigned_DNA.
EMBL; X72872; CAA51386.1; -; Genomic_DNA.
PIR; D70698; D70698.
RefSeq; NP_214520.1; NC_000962.3.
RefSeq; WP_003917265.1; NZ_KK339370.1.
PDB; 3IFZ; X-ray; 2.70 A; A/B=1-501.
PDB; 3ILW; X-ray; 1.60 A; A/B=34-500.
PDB; 3UC1; X-ray; 1.65 A; A=514-838.
PDB; 4G3N; X-ray; 1.40 A; A=512-838.
PDB; 5BS8; X-ray; 2.40 A; A/C=2-500.
PDB; 5BTA; X-ray; 2.55 A; A/C=2-500.
PDB; 5BTC; X-ray; 2.55 A; A/C=2-500.
PDB; 5BTD; X-ray; 2.50 A; A/C=2-500.
PDB; 5BTF; X-ray; 2.61 A; A/C=2-500.
PDB; 5BTG; X-ray; 2.50 A; A/C=2-500.
PDB; 5BTI; X-ray; 2.50 A; A/C=2-500.
PDB; 5BTL; X-ray; 2.50 A; A/C=2-500.
PDB; 5BTN; X-ray; 2.50 A; A/C=2-500.
PDBsum; 3IFZ; -.
PDBsum; 3ILW; -.
PDBsum; 3UC1; -.
PDBsum; 4G3N; -.
PDBsum; 5BS8; -.
PDBsum; 5BTA; -.
PDBsum; 5BTC; -.
PDBsum; 5BTD; -.
PDBsum; 5BTF; -.
PDBsum; 5BTG; -.
PDBsum; 5BTI; -.
PDBsum; 5BTL; -.
PDBsum; 5BTN; -.
ProteinModelPortal; P9WG47; -.
SMR; P9WG47; -.
STRING; 83332.Rv0006; -.
BindingDB; P9WG47; -.
ChEMBL; CHEMBL4165; -.
iPTMnet; P9WG47; -.
PaxDb; P9WG47; -.
PRIDE; P9WG47; -.
EnsemblBacteria; CCP42728; CCP42728; Rv0006.
GeneID; 887105; -.
KEGG; mtu:Rv0006; -.
TubercuList; Rv0006; -.
eggNOG; ENOG4105C24; Bacteria.
eggNOG; COG0188; LUCA.
KO; K02469; -.
PhylomeDB; P9WG47; -.
PRO; PR:P9WG47; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005694; C:chromosome; IEA:InterPro.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0005524; F:ATP binding; IDA:MTBBASE.
GO; GO:0016887; F:ATPase activity; IDA:MTBBASE.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0034335; F:DNA supercoiling activity; IDA:UniProtKB.
GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IDA:MTBBASE.
GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
GO; GO:0006265; P:DNA topological change; IDA:MTBBASE.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
CDD; cd00187; TOP4c; 1.
Gene3D; 1.10.268.10; -; 1.
Gene3D; 2.120.10.90; -; 1.
Gene3D; 3.90.199.10; -; 3.
HAMAP; MF_01897; GyrA; 1.
InterPro; IPR005743; GyrA.
InterPro; IPR006691; GyrA/parC_rep.
InterPro; IPR035516; Gyrase/topoIV_suA_C.
InterPro; IPR013760; Topo_IIA-like_dom_sf.
InterPro; IPR002205; Topo_IIA_A/C.
InterPro; IPR013758; Topo_IIA_A/C_ab.
InterPro; IPR013757; Topo_IIA_A_a_sf.
Pfam; PF03989; DNA_gyraseA_C; 6.
Pfam; PF00521; DNA_topoisoIV; 1.
SMART; SM00434; TOP4c; 1.
SUPFAM; SSF101904; SSF101904; 1.
SUPFAM; SSF56719; SSF56719; 1.
PROSITE; PS00018; EF_HAND_1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Antibiotic resistance; ATP-binding;
Calcium; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
Nucleotide-binding; Reference proteome; Topoisomerase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:21969609}.
CHAIN 2 838 DNA gyrase subunit A.
/FTId=PRO_0000145243.
DOMAIN 504 516 EF-hand. {ECO:0000305|PubMed:22844097}.
CA_BIND 504 516 {ECO:0000305|PubMed:22844097}.
REGION 514 838 C-terminal domain CTD.
{ECO:0000303|PubMed:22457352,
ECO:0000303|PubMed:23869946}.
MOTIF 537 543 GyrA-box. {ECO:0000255|HAMAP-
Rule:MF_01897,
ECO:0000303|PubMed:23869946}.
MOTIF 743 749 GyrA-box-1.
{ECO:0000303|PubMed:23869946}.
ACT_SITE 129 129 O-(5'-phospho-DNA)-tyrosine intermediate.
{ECO:0000255|HAMAP-Rule:MF_01897}.
MOD_RES 2 2 N-acetylthreonine.
{ECO:0000244|PubMed:21969609}.
VARIANT 90 90 A -> V (confers ciprofloxacin resistance,
in clinical isolate).
{ECO:0000269|PubMed:8031045}.
VARIANT 91 91 S -> P (confers ciprofloxacin resistance,
in clinical isolate).
{ECO:0000269|PubMed:8031045}.
VARIANT 94 94 D -> A (confers ciprofloxacin resistance,
in clinical isolate).
{ECO:0000269|PubMed:8031045}.
VARIANT 94 94 D -> G (confers ciprofloxacin resistance,
in clinical isolate).
{ECO:0000269|PubMed:8031045}.
VARIANT 94 94 D -> H (confers ciprofloxacin resistance,
in clinical isolate).
{ECO:0000269|PubMed:8031045}.
VARIANT 94 94 D -> N (confers ciprofloxacin resistance,
in clinical isolate).
{ECO:0000269|PubMed:8031045}.
VARIANT 94 94 D -> Y (confers ciprofloxacin resistance,
in clinical isolate).
{ECO:0000269|PubMed:8031045}.
MUTAGEN 80 80 T->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.
{ECO:0000269|PubMed:16377674}.
MUTAGEN 88 88 G->A: Confers fluoroquinolone resistance,
IC(50) is 2- to 26-fold higher than wild-
type. {ECO:0000269|PubMed:17015625}.
MUTAGEN 88 88 G->C: Confers fluoroquinolone resistance,
IC(50) is 3- to 43-fold higher than wild-
type, in strains H37Ra and H37Rv.
{ECO:0000269|PubMed:17015625,
ECO:0000269|PubMed:8031045}.
MUTAGEN 90 94 ASIYD->VSIYG: 80-fold increased
resistance to fluoroquinolones, 32- to
64-fold reduction in fluoroquinolone-
induced DNA cleavage.
{ECO:0000269|PubMed:16377674}.
MUTAGEN 90 90 A->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.
{ECO:0000269|PubMed:16377674}.
MUTAGEN 90 90 A->S: Increased susceptibility to
fluoroquinolones (makes sequence more
like E.coli), supercoiling, relaxation,
decatenation activities still inhibited
by MfpA. {ECO:0000269|PubMed:18426901,
ECO:0000269|PubMed:19060136}.
MUTAGEN 90 90 A->V: 17-fold increased resistance to
fluoroquinolones, 4- to 8-fold reduction
in fluoroquinolone-induced DNA cleavage.
{ECO:0000269|PubMed:16377674}.
MUTAGEN 94 94 D->G,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.
{ECO:0000269|PubMed:16377674,
ECO:0000269|PubMed:19060136}.
MUTAGEN 94 94 D->H: Confers ofloxacin resistance.
{ECO:0000269|PubMed:8035042}.
MUTAGEN 504 514 DVSDEDLIARE->AVSDAALIARA: Significant
reduction in DNA wrapping and
supercoiling activity, no change in
decatanation or relaxation activities.
{ECO:0000269|PubMed:22844097}.
MUTAGEN 508 509 ED->AA: Slight reduction in supercoiling
activity. {ECO:0000269|PubMed:22844097}.
MUTAGEN 538 538 K->R: Wild-type decatenase activity
(changes residue to match E.coli).
{ECO:0000269|PubMed:23869946}.
MUTAGEN 540 543 GGKG->AAKA: No supercoiling activity,
almost wild-type decatenation activity,
wild-type fluoroquinolone-induced DNA
cleavage. {ECO:0000269|PubMed:23869946}.
MUTAGEN 540 540 G->A: No change in supercoiling activity,
wild-type decatenation or
fluoroquinolone-induced DNA cleavage.
{ECO:0000269|PubMed:23869946}.
MUTAGEN 541 541 G->A: Reduced supercoiling activity,
wild-type decatenation and
fluoroquinolone-induced DNA cleavage.
{ECO:0000269|PubMed:23869946}.
MUTAGEN 543 543 G->A: Reduced supercoiling activity,
wild-type decatenation and
fluoroquinolone-induced DNA cleavage.
{ECO:0000269|PubMed:23869946}.
MUTAGEN 543 543 G->K: No supercoiling activity, wild-type
decatenation and fluoroquinolone-induced
DNA cleavage.
{ECO:0000269|PubMed:23869946}.
MUTAGEN 544 545 VQ->KS: Wild-type decatenase activity
(changes residues to match E.coli).
{ECO:0000269|PubMed:23869946}.
MUTAGEN 746 749 GGKG->AAKA: No supercoiling or
decatenation activity, decreased
fluoroquinolone-induced DNA cleavage.
{ECO:0000269|PubMed:23869946}.
MUTAGEN 746 746 G->A: Wild-type supercoiling,
decatenation and fluoroquinolone-induced
DNA cleavage.
{ECO:0000269|PubMed:23869946}.
MUTAGEN 747 747 G->A: Wild-type supercoiling,
decatenation and fluoroquinolone-induced
DNA cleavage.
{ECO:0000269|PubMed:23869946}.
MUTAGEN 749 749 G->A: No supercoiling or decatenation
activity, decreased fluoroquinolone-
induced DNA cleavage.
{ECO:0000269|PubMed:23869946}.
CONFLICT 83 83 N -> K (in Ref. 4; AAC36878).
{ECO:0000305}.
CONFLICT 712 712 L -> V (in Ref. 1; AAA83017).
{ECO:0000305}.
STRAND 16 19 {ECO:0000244|PDB:5BS8}.
TURN 38 40 {ECO:0000244|PDB:3ILW}.
TURN 44 46 {ECO:0000244|PDB:3ILW}.
HELIX 50 62 {ECO:0000244|PDB:3ILW}.
HELIX 73 83 {ECO:0000244|PDB:3ILW}.
HELIX 91 100 {ECO:0000244|PDB:3ILW}.
TURN 102 104 {ECO:0000244|PDB:3ILW}.
STRAND 109 114 {ECO:0000244|PDB:3ILW}.
STRAND 119 121 {ECO:0000244|PDB:3ILW}.
HELIX 127 129 {ECO:0000244|PDB:5BS8}.
STRAND 131 134 {ECO:0000244|PDB:3ILW}.
HELIX 136 142 {ECO:0000244|PDB:3ILW}.
HELIX 145 147 {ECO:0000244|PDB:3ILW}.
STRAND 152 154 {ECO:0000244|PDB:3ILW}.
STRAND 158 165 {ECO:0000244|PDB:3ILW}.
HELIX 172 176 {ECO:0000244|PDB:3ILW}.
STRAND 178 181 {ECO:0000244|PDB:5BS8}.
STRAND 186 189 {ECO:0000244|PDB:5BS8}.
HELIX 194 206 {ECO:0000244|PDB:3ILW}.
TURN 207 209 {ECO:0000244|PDB:3ILW}.
HELIX 212 222 {ECO:0000244|PDB:3ILW}.
STRAND 233 235 {ECO:0000244|PDB:3ILW}.
HELIX 238 246 {ECO:0000244|PDB:3ILW}.
STRAND 247 254 {ECO:0000244|PDB:3ILW}.
STRAND 256 261 {ECO:0000244|PDB:3ILW}.
STRAND 263 265 {ECO:0000244|PDB:5BS8}.
STRAND 267 273 {ECO:0000244|PDB:3ILW}.
HELIX 280 292 {ECO:0000244|PDB:3ILW}.
STRAND 299 304 {ECO:0000244|PDB:3ILW}.
TURN 308 310 {ECO:0000244|PDB:3ILW}.
STRAND 314 318 {ECO:0000244|PDB:3ILW}.
HELIX 324 334 {ECO:0000244|PDB:3ILW}.
STRAND 338 344 {ECO:0000244|PDB:3ILW}.
STRAND 346 349 {ECO:0000244|PDB:3ILW}.
STRAND 352 355 {ECO:0000244|PDB:3ILW}.
HELIX 358 399 {ECO:0000244|PDB:3ILW}.
HELIX 401 410 {ECO:0000244|PDB:3ILW}.
HELIX 414 425 {ECO:0000244|PDB:3ILW}.
HELIX 429 436 {ECO:0000244|PDB:3ILW}.
HELIX 440 443 {ECO:0000244|PDB:3ILW}.
HELIX 445 470 {ECO:0000244|PDB:3ILW}.
HELIX 472 490 {ECO:0000244|PDB:3ILW}.
STRAND 496 499 {ECO:0000244|PDB:3ILW}.
STRAND 515 521 {ECO:0000244|PDB:4G3N}.
STRAND 524 530 {ECO:0000244|PDB:4G3N}.
HELIX 531 534 {ECO:0000244|PDB:4G3N}.
HELIX 551 553 {ECO:0000244|PDB:4G3N}.
STRAND 555 562 {ECO:0000244|PDB:4G3N}.
STRAND 565 571 {ECO:0000244|PDB:4G3N}.
STRAND 574 580 {ECO:0000244|PDB:4G3N}.
HELIX 581 583 {ECO:0000244|PDB:4G3N}.
STRAND 589 591 {ECO:0000244|PDB:3UC1}.
HELIX 596 599 {ECO:0000244|PDB:4G3N}.
STRAND 608 616 {ECO:0000244|PDB:4G3N}.
STRAND 619 627 {ECO:0000244|PDB:4G3N}.
STRAND 630 636 {ECO:0000244|PDB:4G3N}.
HELIX 637 640 {ECO:0000244|PDB:4G3N}.
STRAND 645 650 {ECO:0000244|PDB:4G3N}.
STRAND 659 665 {ECO:0000244|PDB:4G3N}.
STRAND 670 675 {ECO:0000244|PDB:4G3N}.
STRAND 678 684 {ECO:0000244|PDB:4G3N}.
TURN 687 689 {ECO:0000244|PDB:4G3N}.
STRAND 695 697 {ECO:0000244|PDB:4G3N}.
STRAND 700 702 {ECO:0000244|PDB:4G3N}.
STRAND 711 716 {ECO:0000244|PDB:4G3N}.
STRAND 722 727 {ECO:0000244|PDB:4G3N}.
STRAND 730 736 {ECO:0000244|PDB:4G3N}.
HELIX 737 739 {ECO:0000244|PDB:4G3N}.
STRAND 750 753 {ECO:0000244|PDB:4G3N}.
TURN 757 759 {ECO:0000244|PDB:4G3N}.
STRAND 762 768 {ECO:0000244|PDB:4G3N}.
STRAND 773 781 {ECO:0000244|PDB:4G3N}.
STRAND 783 787 {ECO:0000244|PDB:4G3N}.
HELIX 788 790 {ECO:0000244|PDB:4G3N}.
STRAND 812 818 {ECO:0000244|PDB:4G3N}.
SEQUENCE 838 AA; 92274 MW; 84DAFE13D74D76D7 CRC64;
MTDTTLPPDD SLDRIEPVDI EQEMQRSYID YAMSVIVGRA LPEVRDGLKP VHRRVLYAMF
DSGFRPDRSH AKSARSVAET MGNYHPHGDA SIYDSLVRMA QPWSLRYPLV DGQGNFGSPG
NDPPAAMRYT EARLTPLAME MLREIDEETV DFIPNYDGRV QEPTVLPSRF PNLLANGSGG
IAVGMATNIP PHNLRELADA VFWALENHDA DEEETLAAVM GRVKGPDFPT AGLIVGSQGT
ADAYKTGRGS IRMRGVVEVE EDSRGRTSLV ITELPYQVNH DNFITSIAEQ VRDGKLAGIS
NIEDQSSDRV GLRIVIEIKR DAVAKVVINN LYKHTQLQTS FGANMLAIVD GVPRTLRLDQ
LIRYYVDHQL DVIVRRTTYR LRKANERAHI LRGLVKALDA LDEVIALIRA SETVDIARAG
LIELLDIDEI QAQAILDMQL RRLAALERQR IIDDLAKIEA EIADLEDILA KPERQRGIVR
DELAEIVDRH GDDRRTRIIA ADGDVSDEDL IAREDVVVTI TETGYAKRTK TDLYRSQKRG
GKGVQGAGLK QDDIVAHFFV CSTHDLILFF TTQGRVYRAK AYDLPEASRT ARGQHVANLL
AFQPEERIAQ VIQIRGYTDA PYLVLATRNG LVKKSKLTDF DSNRSGGIVA VNLRDNDELV
GAVLCSAGDD LLLVSANGQS IRFSATDEAL RPMGRATSGV QGMRFNIDDR LLSLNVVREG
TYLLVATSGG YAKRTAIEEY PVQGRGGKGV LTVMYDRRRG RLVGALIVDD DSELYAVTSG
GGVIRTAARQ VRKAGRQTKG VRLMNLGEGD TLLAIARNAE ESGDDNAVDA NGADQTGN


Related products :

Catalog number Product name Quantity
EIAAB32718 HC9,Homo sapiens,Human,Macropain subunit C9,Multicatalytic endopeptidase complex subunit C9,Proteasome component C9,Proteasome subunit alpha type-4,Proteasome subunit L,PSC9,PSMA4
EIAAB32716 Macropain subunit C9,Multicatalytic endopeptidase complex subunit C9,Proteasome component C9,Proteasome subunit alpha type-4,Proteasome subunit L,Psma4,Rat,Rattus norvegicus
EIAAB32715 Macropain subunit C9,Mouse,Multicatalytic endopeptidase complex subunit C9,Mus musculus,Proteasome component C9,Proteasome subunit alpha type-4,Proteasome subunit L,Psma4
EIAAB32714 Macropain subunit C8,Mouse,Multicatalytic endopeptidase complex subunit C8,Mus musculus,Proteasome component C8,Proteasome subunit alpha type-3,Proteasome subunit K,Psma3
EIAAB32711 Macropain subunit C8,Multicatalytic endopeptidase complex subunit C8,Proteasome component C8,Proteasome subunit alpha type-3,Proteasome subunit K,Psma3,Rat,Rattus norvegicus
EIAAB32776 Homo sapiens,Human,LMP7,Low molecular mass protein 7,Macropain subunit C13,Multicatalytic endopeptidase complex subunit C13,Proteasome component C13,Proteasome subunit beta type-8,Proteasome subunit b
EIAAB45652 Atp6a1,Atp6a2,Atp6v1a,Atp6v1a1,Mouse,Mus musculus,Vacuolar proton pump subunit alpha,V-ATPase 69 kDa subunit,V-ATPase subunit A,V-type proton ATPase catalytic subunit A
EIAAB45577 ATP6V0E2,ATP6V0E2L,C7orf32,Homo sapiens,Human,Lysosomal 9 kDa H(+)-transporting ATPase V0 subunit e2,Vacuolar proton pump subunit e 2,V-ATPase subunit e 2,V-type proton ATPase subunit e 2
orb60899 Nalidixic acid Nalidixic acid(NegGram) is a synthetic 1,8-naphthyridine antimicrobial agent with a limited bacteriocidal spectrum. It is an inhibitor of the A subunit of bacterial DNA gyrase. For rese 10 mg
EIAAB45686 ATP6G,ATP6G2,ATP6V1G2,Homo sapiens,Human,NG38,Vacuolar proton pump subunit G 2,V-ATPase 13 kDa subunit 2,V-ATPase subunit G 2,V-type proton ATPase subunit G 2
EIAAB45651 ATP6A1,ATP6V1A,ATP6V1A1,Bos taurus,Bovine,Vacuolar proton pump subunit alpha,V-ATPase 69 kDa subunit,V-ATPase subunit A,V-type proton ATPase catalytic subunit A
EIAAB45650 ATP6A1,ATP6V1A,ATP6V1A1,Pig,Sus scrofa,Vacuolar proton pump subunit alpha,V-ATPase 69 kDa subunit,V-ATPase subunit A,V-type proton ATPase catalytic subunit A
EIAAB45678 ATP6S14,ATP6V1F,Homo sapiens,Human,Vacuolar proton pump subunit F,VATF,V-ATPase 14 kDa subunit,V-ATPase subunit F,V-type proton ATPase subunit F
EIAAB45673 ATP6E,ATP6E2,ATP6V1E1,Homo sapiens,Human,p31,Vacuolar proton pump subunit E 1,V-ATPase 31 kDa subunit,V-ATPase subunit E 1,V-type proton ATPase subunit E 1
EIAAB32777 Macropain subunit C13,Multicatalytic endopeptidase complex subunit C13,Proteasome component C13,Proteasome subunit beta type-8,Proteasome subunit beta-5i,Psmb8,Rat,Rattus norvegicus
EIAAB45680 Atp6s14,Atp6v1f,Rat,Rattus norvegicus,Vacuolar proton pump subunit F,Vatf,V-ATPase 14 kDa subunit,V-ATPase subunit F,V-type proton ATPase subunit F
EIAAB45679 Atp6s14,Atp6v1f,Mouse,Mus musculus,Vacuolar proton pump subunit F,Vatf,V-ATPase 14 kDa subunit,V-ATPase subunit F,V-type proton ATPase subunit F
EIAAB45681 ATP6S14,ATP6V1F,Bos taurus,Bovine,Vacuolar proton pump subunit F,VATF,V-ATPase 14 kDa subunit,V-ATPase subunit F,V-type proton ATPase subunit F
EIAAB32773 Macropain subunit C13,Multicatalytic endopeptidase complex subunit C13,Pig,Proteasome component C13,Proteasome subunit beta type-8,Proteasome subunit beta-5i,PSMB8,Sus scrofa
EIAAB45672 Atp6e,Atp6e2,Atp6v1e1,Mouse,Mus musculus,p31,Vacuolar proton pump subunit E 1,V-ATPase 31 kDa subunit,V-ATPase subunit E 1,V-type proton ATPase subunit E 1
EIAAB45688 Atp6g2,Atp6v1g2,Mouse,Mus musculus,Ng38,Vacuolar proton pump subunit G 2,V-ATPase 13 kDa subunit 2,V-ATPase subunit G 2,V-type proton ATPase subunit G 2
EIAAB45689 ATP6G3,ATP6V1G3,Homo sapiens,Human,Vacuolar proton pump subunit G 3,V-ATPase 13 kDa subunit 3,V-ATPase subunit G 3,V-type proton ATPase subunit G 3
EIAAB45573 ATP6H,ATP6V0E,ATP6V0E1,Homo sapiens,Human,Vacuolar proton pump subunit e 1,V-ATPase 9.2 kDa membrane accessory protein,V-ATPase M9.2 subunit,V-ATPase subunit e 1,V-type proton ATPase subunit e 1
EIAAB45629 ATP6AP1,ATP6IP1,ATP6S1,Bos taurus,Bovine,Vacuolar proton pump subunit S1,V-ATPase Ac45 subunit,V-ATPase S1 accessory protein,V-ATPase subunit S1,V-type proton ATPase subunit S1
EIAAB45562 Atp6d,Atp6v0d1,Mouse,Mus musculus,P39,Physophilin,Vacuolar proton pump subunit d 1,V-ATPase 40 kDa accessory protein,V-ATPase AC39 subunit,V-ATPase subunit d 1,V-type proton ATPase subunit d 1


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur