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DNA gyrase subunit B (EC 5.99.1.3)

 GYRB_MYCTU              Reviewed;         675 AA.
P9WG45; L0T585; P0C5C5; P41514; P77897;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
12-SEP-2018, entry version 33.
RecName: Full=DNA gyrase subunit B {ECO:0000255|HAMAP-Rule:MF_01898};
EC=5.99.1.3 {ECO:0000255|HAMAP-Rule:MF_01898, ECO:0000269|PubMed:15047530, ECO:0000269|PubMed:16876125};
Name=gyrB {ECO:0000255|HAMAP-Rule:MF_01898}; OrderedLocusNames=Rv0005;
ORFNames=MTCY10H4.03;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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]
SEQUENCE REVISION TO 513-518.
Telenti A.;
Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
[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]
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).
[5]
FUNCTION, MUTAGENESIS OF ASP-472 AND ASN-499, 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).
[6]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, 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).
[7]
FUNCTION, MUTAGENESIS OF ARG-482, 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).
[8]
FUNCTION, AND ACTIVITY REGULATION.
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).
[9]
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).
[10]
FUNCTION.
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).
[11]
FUNCTION, AND COFACTOR.
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).
[12]
ACTIVITY REGULATION, MUTAGENESIS OF GLY-157, AND ANTIBIOTIC
RESISTANCE.
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).
[13]
FUNCTION.
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).
[14]
ACTIVITY REGULATION, AND MUTAGENESIS OF SER-169.
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).
[15]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 448-675, FUNCTION, DOMAIN,
AND MUTAGENESIS OF ASP-577; 620-GLU--ASP-627; GLU-620; GLU-623 AND
ASP-627.
PubMed=19596812; DOI=10.1093/nar/gkp586;
Fu G., Wu J., Liu W., Zhu D., Hu Y., Deng J., Zhang X.E., Bi L.,
Wang D.C.;
"Crystal structure of DNA gyrase B' domain sheds lights on the
mechanism for T-segment navigation.";
Nucleic Acids Res. 37:5908-5916(2009).
[16]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 448-675, 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).
[17]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 2-427 IN COMPLEX WITH ATP
ANALOGS AND MAGNESIUM, FUNCTION, AND ATP-BINDING.
STRAIN=H37Rv;
PubMed=24015710; DOI=10.1042/BJ20130538;
Agrawal A., Roue M., Spitzfaden C., Petrella S., Aubry A., Hann M.,
Bax B., Mayer C.;
"Mycobacterium tuberculosis DNA gyrase ATPase domain structures
suggest a dissociative mechanism that explains how ATP hydrolysis is
coupled to domain motion.";
Biochem. J. 456:263-273(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:16876125, PubMed:19060136, PubMed:16377674,
PubMed:18426901, PubMed:22844097, PubMed:19596812,
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, PubMed:24015710).
{ECO:0000269|PubMed:15047530, ECO:0000269|PubMed:16377674,
ECO:0000269|PubMed:16876125, ECO:0000269|PubMed:18426901,
ECO:0000269|PubMed:19060136, ECO:0000269|PubMed:19596812,
ECO:0000269|PubMed:20805881, ECO:0000269|PubMed:22457352,
ECO:0000269|PubMed:22844097, ECO:0000269|PubMed:23869946,
ECO:0000269|PubMed:24015710}.
-!- 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_01898,
ECO:0000269|PubMed:15047530, ECO:0000269|PubMed:16876125}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_01898,
ECO:0000269|PubMed:16876125, ECO:0000269|PubMed:24015710};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000255|HAMAP-Rule:MF_01898};
Note=Mg(2+) required for DNA supercoiling, DNA relaxation, DNA
cleavage and DNA decatenation, Mn(2+) substitutes for relaxation
but not supercoiling or cleavage activity (PubMed:16876125).
Ca(2+) does not substitute for supercoiling activity
(PubMed:22844097). {ECO:0000269|PubMed:16876125,
ECO:0000269|PubMed:22844097};
-!- ACTIVITY REGULATION: DNA supercoiling inhibited by
(fluoro)quinoline antibiotics such as sparfloxacin and
levofloxacin, which usually act on GyrA subunit (PubMed:15047530).
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:19060136,
ECO:0000269|PubMed:23268609, ECO:0000269|PubMed:23869946,
ECO:0000269|PubMed:24126580}.
-!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains
(PubMed:15047530). 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.
{ECO:0000255|HAMAP-Rule:MF_01898, ECO:0000269|PubMed:15047530}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01898}.
-!- DOMAIN: The B' domain (residues 448-675, Toprim plus a tail
domain) forms a dimer; when reconstituted with intact GyrA the
complex has ATP-independent DNA relaxation activity
(PubMed:19596812). The same fragment (also called TopBK) when
reconstituted with intact GyrA or the N-terminus of GyrA (residues
1-502) can catalyze quinolone-mediated DNA breaks
(PubMed:20805881). {ECO:0000269|PubMed:19596812,
ECO:0000269|PubMed:20805881}.
-!- 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:16876125, 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 the GyrA subunit) (PubMed:18426901).
{ECO:0000269|PubMed:18426901, ECO:0000305|PubMed:15047530,
ECO:0000305|PubMed:16377674, ECO:0000305|PubMed:16876125,
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}.
-!- MISCELLANEOUS: Few gyrases are as efficient as E.coli at forming
negative supercoils. 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.
{ECO:0000255|HAMAP-Rule:MF_01898}.
-!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
{ECO:0000255|HAMAP-Rule:MF_01898}.
-!- SEQUENCE CAUTION:
Sequence=AAA83016.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; L27512; AAA83016.1; ALT_INIT; Genomic_DNA.
EMBL; AL123456; CCP42727.1; -; Genomic_DNA.
PIR; S44198; S44198.
RefSeq; NP_214519.2; NC_000962.3.
RefSeq; WP_003917863.1; NZ_KK339370.1.
PDB; 2ZJT; X-ray; 2.80 A; A/B=448-675.
PDB; 3IG0; X-ray; 2.10 A; A=448-675.
PDB; 3M4I; X-ray; 1.95 A; A=448-675.
PDB; 3ZKB; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=2-427.
PDB; 3ZKD; X-ray; 2.95 A; A/B/C/D/E/F/G/H=2-427.
PDB; 3ZM7; X-ray; 3.30 A; A/B/C/D/E/F=2-428.
PDB; 5BS8; X-ray; 2.40 A; B/D=426-675.
PDB; 5BTA; X-ray; 2.55 A; B/D=426-675.
PDB; 5BTC; X-ray; 2.55 A; B/D=426-675.
PDB; 5BTD; X-ray; 2.50 A; B/D=426-675.
PDB; 5BTF; X-ray; 2.61 A; B/D=426-675.
PDB; 5BTG; X-ray; 2.50 A; B/D=426-675.
PDB; 5BTI; X-ray; 2.50 A; B/D=426-675.
PDB; 5BTL; X-ray; 2.50 A; B/D=426-675.
PDB; 5BTN; X-ray; 2.50 A; B/D=426-675.
PDBsum; 2ZJT; -.
PDBsum; 3IG0; -.
PDBsum; 3M4I; -.
PDBsum; 3ZKB; -.
PDBsum; 3ZKD; -.
PDBsum; 3ZM7; -.
PDBsum; 5BS8; -.
PDBsum; 5BTA; -.
PDBsum; 5BTC; -.
PDBsum; 5BTD; -.
PDBsum; 5BTF; -.
PDBsum; 5BTG; -.
PDBsum; 5BTI; -.
PDBsum; 5BTL; -.
PDBsum; 5BTN; -.
ProteinModelPortal; P9WG45; -.
SMR; P9WG45; -.
STRING; 83332.Rv0005; -.
PaxDb; P9WG45; -.
PRIDE; P9WG45; -.
EnsemblBacteria; CCP42727; CCP42727; Rv0005.
GeneID; 887081; -.
KEGG; mtu:Rv0005; -.
TubercuList; Rv0005; -.
eggNOG; ENOG4105C7D; Bacteria.
eggNOG; COG0187; LUCA.
KO; K02470; -.
OMA; DCSSRDP; -.
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:0009295; C:nucleoid; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0005524; F:ATP binding; 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:0007059; P:chromosome segregation; IBA:GO_Central.
GO; GO:0006265; P:DNA topological change; IBA:GO_Central.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
CDD; cd00075; HATPase_c; 1.
CDD; cd03366; TOPRIM_TopoIIA_GyrB; 1.
Gene3D; 3.30.230.10; -; 1.
Gene3D; 3.30.565.10; -; 1.
Gene3D; 3.40.50.670; -; 1.
HAMAP; MF_01898; GyrB; 1.
InterPro; IPR002288; DNA_gyrase_B_C.
InterPro; IPR011557; GyrB.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
InterPro; IPR001241; Topo_IIA.
InterPro; IPR013760; Topo_IIA-like_dom_sf.
InterPro; IPR013759; Topo_IIA_B_C.
InterPro; IPR013506; Topo_IIA_bsu_dom2.
InterPro; IPR018522; TopoIIA_CS.
InterPro; IPR006171; TOPRIM_domain.
InterPro; IPR034160; TOPRIM_GyrB.
PANTHER; PTHR10169; PTHR10169; 1.
Pfam; PF00204; DNA_gyraseB; 1.
Pfam; PF00986; DNA_gyraseB_C; 1.
Pfam; PF02518; HATPase_c; 1.
Pfam; PF01751; Toprim; 1.
SMART; SM00387; HATPase_c; 1.
SMART; SM00433; TOP2c; 1.
SUPFAM; SSF54211; SSF54211; 1.
SUPFAM; SSF55874; SSF55874; 1.
SUPFAM; SSF56719; SSF56719; 1.
TIGRFAMs; TIGR01059; gyrB; 1.
PROSITE; PS00177; TOPOISOMERASE_II; 1.
PROSITE; PS50880; TOPRIM; 1.
1: Evidence at protein level;
3D-structure; Antibiotic resistance; ATP-binding; Complete proteome;
Cytoplasm; DNA-binding; Isomerase; Magnesium; Metal-binding;
Nucleotide-binding; Reference proteome; Topoisomerase.
CHAIN 1 675 DNA gyrase subunit B.
/FTId=PRO_0000145325.
DOMAIN 453 567 Toprim. {ECO:0000255|HAMAP-
Rule:MF_01898}.
NP_BIND 107 108 ATP. {ECO:0000269|PubMed:24015710}.
NP_BIND 120 125 ATP. {ECO:0000269|PubMed:24015710}.
NP_BIND 370 372 ATP. {ECO:0000269|PubMed:24015710}.
METAL 459 459 Magnesium 1; catalytic.
{ECO:0000255|HAMAP-Rule:MF_01898}.
METAL 532 532 Magnesium 1; catalytic.
{ECO:0000255|HAMAP-Rule:MF_01898}.
METAL 532 532 Magnesium 2. {ECO:0000255|HAMAP-
Rule:MF_01898}.
METAL 534 534 Magnesium 2. {ECO:0000255|HAMAP-
Rule:MF_01898}.
BINDING 12 12 ATP. {ECO:0000269|PubMed:24015710}.
BINDING 52 52 ATP. {ECO:0000269|PubMed:24015710}.
BINDING 79 79 ATP. {ECO:0000269|PubMed:24015710}.
BINDING 83 83 ATP; via carbonyl oxygen.
{ECO:0000269|PubMed:24015710}.
BINDING 114 114 ATP. {ECO:0000269|PubMed:24015710}.
BINDING 169 169 ATP. {ECO:0000269|PubMed:24015710}.
SITE 484 484 Interaction with DNA. {ECO:0000255|HAMAP-
Rule:MF_01898}.
SITE 487 487 Interaction with DNA. {ECO:0000255|HAMAP-
Rule:MF_01898}.
MUTAGEN 157 157 G->S: Increased resistance to
aminopyrazinamides, however genome not
sequenced. {ECO:0000269|PubMed:23268609}.
MUTAGEN 169 169 S->A: Increased resistance to
pyrrolamides and novobiocin, however
genome not sequenced.
{ECO:0000269|PubMed:24126580}.
MUTAGEN 472 472 D->H: No supercoiling activity.
{ECO:0000269|PubMed:16377674}.
MUTAGEN 482 482 R->K: Increased susceptibility to
fluoroquinolones, half supercoiling
activity, no fluoroquinolone-induced DNA
cleavage (makes sequence more like
E.coli). {ECO:0000269|PubMed:18426901}.
MUTAGEN 499 499 N->D: 17-fold increased resistance to
fluoroquinolones, slightly increased DNA
cleavage in absence of drugs.
{ECO:0000269|PubMed:16377674}.
MUTAGEN 577 577 D->A: 37% supercoiling, 54% decatenation,
126% DNA cleavage in presence of
norfloxacin.
{ECO:0000269|PubMed:19596812}.
MUTAGEN 577 577 D->R: <2% supercoiling, 4% decatenation.
{ECO:0000269|PubMed:19596812}.
MUTAGEN 620 627 ELWETTMD->ALWETTMA: <3% supercoiling, 18%
decatenation, 75% DNA cleavage in
presence of norfloxacin.
{ECO:0000269|PubMed:19596812}.
MUTAGEN 620 620 E->A: 15% supercoiling, 19% decatenation,
143% DNA cleavage in presence of
norfloxacin.
{ECO:0000269|PubMed:19596812}.
MUTAGEN 620 620 E->R: 10% supercoiling, 7% decatenation.
{ECO:0000269|PubMed:19596812}.
MUTAGEN 623 623 E->A: 18% supercoiling, 11% decatenation,
131% DNA cleavage in presence of
norfloxacin.
{ECO:0000269|PubMed:19596812}.
MUTAGEN 623 623 E->R: <2% supercoiling, 2% decatenation.
{ECO:0000269|PubMed:19596812}.
MUTAGEN 627 627 D->A: 13% supercoiling, 10% decatenation,
42% DNA cleavage in presence of
norfloxacin.
{ECO:0000269|PubMed:19596812}.
MUTAGEN 627 627 D->R: <2% supercoiling, 3% decatenation.
{ECO:0000269|PubMed:19596812}.
CONFLICT 291 292 MQ -> IE (in Ref. 1; AAA83016).
{ECO:0000305}.
HELIX 14 16 {ECO:0000244|PDB:3ZKB}.
HELIX 24 28 {ECO:0000244|PDB:3ZKB}.
HELIX 31 34 {ECO:0000244|PDB:3ZKB}.
HELIX 39 58 {ECO:0000244|PDB:3ZKB}.
STRAND 64 69 {ECO:0000244|PDB:3ZKB}.
STRAND 75 79 {ECO:0000244|PDB:3ZKB}.
STRAND 92 94 {ECO:0000244|PDB:3ZKB}.
HELIX 95 101 {ECO:0000244|PDB:3ZKB}.
STRAND 105 107 {ECO:0000244|PDB:3ZKB}.
STRAND 109 113 {ECO:0000244|PDB:3ZKB}.
HELIX 124 130 {ECO:0000244|PDB:3ZKB}.
STRAND 132 141 {ECO:0000244|PDB:3ZKB}.
STRAND 144 151 {ECO:0000244|PDB:3ZKB}.
STRAND 159 163 {ECO:0000244|PDB:3ZKB}.
STRAND 168 175 {ECO:0000244|PDB:3ZKB}.
TURN 177 179 {ECO:0000244|PDB:3ZKB}.
HELIX 187 199 {ECO:0000244|PDB:3ZKB}.
STRAND 205 210 {ECO:0000244|PDB:3ZKB}.
HELIX 236 241 {ECO:0000244|PDB:3ZKD}.
STRAND 247 251 {ECO:0000244|PDB:3ZKB}.
TURN 254 256 {ECO:0000244|PDB:3ZKB}.
HELIX 257 264 {ECO:0000244|PDB:3ZKB}.
TURN 265 267 {ECO:0000244|PDB:3ZKB}.
STRAND 270 274 {ECO:0000244|PDB:3ZKD}.
STRAND 276 282 {ECO:0000244|PDB:3ZKB}.
STRAND 285 298 {ECO:0000244|PDB:3ZKB}.
STRAND 300 305 {ECO:0000244|PDB:3ZKB}.
HELIX 315 334 {ECO:0000244|PDB:3ZKB}.
HELIX 347 351 {ECO:0000244|PDB:3ZKB}.
STRAND 354 360 {ECO:0000244|PDB:3ZKB}.
TURN 369 372 {ECO:0000244|PDB:3ZKB}.
HELIX 378 398 {ECO:0000244|PDB:3ZKB}.
HELIX 400 422 {ECO:0000244|PDB:3ZKB}.
HELIX 450 452 {ECO:0000244|PDB:3M4I}.
STRAND 453 462 {ECO:0000244|PDB:3M4I}.
STRAND 475 481 {ECO:0000244|PDB:3M4I}.
TURN 488 490 {ECO:0000244|PDB:5BS8}.
HELIX 493 496 {ECO:0000244|PDB:3M4I}.
HELIX 500 509 {ECO:0000244|PDB:3M4I}.
HELIX 514 516 {ECO:0000244|PDB:3M4I}.
HELIX 519 521 {ECO:0000244|PDB:3M4I}.
STRAND 525 530 {ECO:0000244|PDB:3M4I}.
HELIX 535 551 {ECO:0000244|PDB:3M4I}.
HELIX 554 557 {ECO:0000244|PDB:3M4I}.
STRAND 561 564 {ECO:0000244|PDB:3M4I}.
STRAND 568 571 {ECO:0000244|PDB:3M4I}.
STRAND 573 576 {ECO:0000244|PDB:5BS8}.
STRAND 579 583 {ECO:0000244|PDB:3M4I}.
HELIX 584 597 {ECO:0000244|PDB:3M4I}.
TURN 603 605 {ECO:0000244|PDB:3M4I}.
STRAND 606 609 {ECO:0000244|PDB:3M4I}.
HELIX 613 615 {ECO:0000244|PDB:3M4I}.
HELIX 618 625 {ECO:0000244|PDB:3M4I}.
TURN 628 630 {ECO:0000244|PDB:3M4I}.
STRAND 633 635 {ECO:0000244|PDB:3M4I}.
HELIX 638 653 {ECO:0000244|PDB:3M4I}.
HELIX 656 666 {ECO:0000244|PDB:5BS8}.
HELIX 667 672 {ECO:0000244|PDB:5BS8}.
SEQUENCE 675 AA; 74091 MW; 4559D0D3FDAC8DC1 CRC64;
MAAQKKKAQD EYGAASITIL EGLEAVRKRP GMYIGSTGER GLHHLIWEVV DNAVDEAMAG
YATTVNVVLL EDGGVEVADD GRGIPVATHA SGIPTVDVVM TQLHAGGKFD SDAYAISGGL
HGVGVSVVNA LSTRLEVEIK RDGYEWSQVY EKSEPLGLKQ GAPTKKTGST VRFWADPAVF
ETTEYDFETV ARRLQEMAFL NKGLTINLTD ERVTQDEVVD EVVSDVAEAP KSASERAAES
TAPHKVKSRT FHYPGGLVDF VKHINRTKNA IHSSIVDFSG KGTGHEVEIA MQWNAGYSES
VHTFANTINT HEGGTHEEGF RSALTSVVNK YAKDRKLLKD KDPNLTGDDI REGLAAVISV
KVSEPQFEGQ TKTKLGNTEV KSFVQKVCNE QLTHWFEANP TDAKVVVNKA VSSAQARIAA
RKARELVRRK SATDIGGLPG KLADCRSTDP RKSELYVVEG DSAGGSAKSG RDSMFQAILP
LRGKIINVEK ARIDRVLKNT EVQAIITALG TGIHDEFDIG KLRYHKIVLM ADADVDGQHI
STLLLTLLFR FMRPLIENGH VFLAQPPLYK LKWQRSDPEF AYSDRERDGL LEAGLKAGKK
INKEDGIQRY KGLGEMDAKE LWETTMDPSV RVLRQVTLDD AAAADELFSI LMGEDVDARR
SFITRNAKDV RFLDV


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