GYRB_MYCTU
ID GYRB_MYCTU Reviewed; 675 AA.
AC P9WG45; L0T585; P0C5C5; P41514; P77897;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=DNA gyrase subunit B {ECO:0000255|HAMAP-Rule:MF_01898};
DE EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_01898, ECO:0000269|PubMed:15047530, ECO:0000269|PubMed:16876125};
GN Name=gyrB {ECO:0000255|HAMAP-Rule:MF_01898}; OrderedLocusNames=Rv0005;
GN ORFNames=MTCY10H4.03;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=8031045; DOI=10.1128/aac.38.4.773;
RA Takiff H.E., Salazar L., Guerrero C., Philipp W., Huang W.M.,
RA Kreiswirth B., Cole S.T., Jacobs W.R. Jr., Telenti A.;
RT "Cloning and nucleotide sequence of Mycobacterium tuberculosis gyrA and
RT gyrB genes and detection of quinolone resistance mutations.";
RL Antimicrob. Agents Chemother. 38:773-780(1994).
RN [2]
RP SEQUENCE REVISION TO 513-518.
RA Telenti A.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND REACTION
RP MECHANISM.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15047530; DOI=10.1128/aac.48.4.1281-1288.2004;
RA Aubry A., Pan X.S., Fisher L.M., Jarlier V., Cambau E.;
RT "Mycobacterium tuberculosis DNA gyrase: interaction with quinolones and
RT correlation with antimycobacterial drug activity.";
RL Antimicrob. Agents Chemother. 48:1281-1288(2004).
RN [5]
RP FUNCTION, MUTAGENESIS OF ASP-472 AND ASN-499, AND ANTIBIOTIC RESISTANCE.
RC STRAIN=H37Rv;
RX PubMed=16377674; DOI=10.1128/aac.50.1.104-112.2006;
RA Aubry A., Veziris N., Cambau E., Truffot-Pernot C., Jarlier V.,
RA Fisher L.M.;
RT "Novel gyrase mutations in quinolone-resistant and -hypersusceptible
RT clinical isolates of Mycobacterium tuberculosis: functional analysis of
RT mutant enzymes.";
RL Antimicrob. Agents Chemother. 50:104-112(2006).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND ACTIVITY REGULATION.
RC STRAIN=H37Rv;
RX PubMed=16876125; DOI=10.1016/j.bbrc.2006.07.017;
RA Aubry A., Fisher L.M., Jarlier V., Cambau E.;
RT "First functional characterization of a singly expressed bacterial type II
RT topoisomerase: the enzyme from Mycobacterium tuberculosis.";
RL Biochem. Biophys. Res. Commun. 348:158-165(2006).
RN [7]
RP FUNCTION, MUTAGENESIS OF ARG-482, AND ANTIBIOTIC SUSCEPTIBILITY.
RX PubMed=18426901; DOI=10.1128/aac.01380-07;
RA Matrat S., Aubry A., Mayer C., Jarlier V., Cambau E.;
RT "Mutagenesis in the alpha3alpha4 GyrA helix and in the Toprim domain of
RT GyrB refines the contribution of Mycobacterium tuberculosis DNA gyrase to
RT intrinsic resistance to quinolones.";
RL Antimicrob. Agents Chemother. 52:2909-2914(2008).
RN [8]
RP FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=H37Rv;
RX PubMed=19060136; DOI=10.1128/jb.01205-08;
RA Merens A., Matrat S., Aubry A., Lascols C., Jarlier V., Soussy C.J.,
RA Cavallo J.D., Cambau E.;
RT "The pentapeptide repeat proteins MfpAMt and QnrB4 exhibit opposite effects
RT on DNA gyrase catalytic reactions and on the ternary gyrase-DNA-quinolone
RT complex.";
RL J. Bacteriol. 191:1587-1594(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [10]
RP FUNCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=22457352; DOI=10.1074/jbc.m112.345736;
RA Tretter E.M., Berger J.M.;
RT "Mechanisms for defining supercoiling set point of DNA gyrase orthologs:
RT II. The shape of the GyrA subunit C-terminal domain (CTD) is not a sole
RT determinant for controlling supercoiling efficiency.";
RL J. Biol. Chem. 287:18645-18654(2012).
RN [11]
RP FUNCTION, AND COFACTOR.
RX PubMed=22844097; DOI=10.1093/nar/gks704;
RA Karkare S., Yousafzai F., Mitchenall L.A., Maxwell A.;
RT "The role of Ca(2+) in the activity of Mycobacterium tuberculosis DNA
RT gyrase.";
RL Nucleic Acids Res. 40:9774-9787(2012).
RN [12]
RP ACTIVITY REGULATION, MUTAGENESIS OF GLY-157, AND ANTIBIOTIC RESISTANCE.
RC STRAIN=H37Rv;
RX PubMed=23268609; DOI=10.1021/cb300510w;
RA Shirude P.S., Madhavapeddi P., Tucker J.A., Murugan K., Patil V.,
RA Basavarajappa H., Raichurkar A.V., Humnabadkar V., Hussein S., Sharma S.,
RA Ramya V.K., Narayan C.B., Balganesh T.S., Sambandamurthy V.K.;
RT "Aminopyrazinamides: novel and specific GyrB inhibitors that kill
RT replicating and nonreplicating Mycobacterium tuberculosis.";
RL ACS Chem. Biol. 8:519-523(2013).
RN [13]
RP FUNCTION.
RC STRAIN=H37Rv;
RX PubMed=23869946; DOI=10.1042/bj20130430;
RA Bouige A., Darmon A., Piton J., Roue M., Petrella S., Capton E.,
RA Forterre P., Aubry A., Mayer C.;
RT "Mycobacterium tuberculosis DNA gyrase possesses two functional GyrA-
RT boxes.";
RL Biochem. J. 455:285-294(2013).
RN [14]
RP ACTIVITY REGULATION, AND MUTAGENESIS OF SER-169.
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RX PubMed=24126580; DOI=10.1128/aac.01751-13;
RA P S.H., Solapure S., Mukherjee K., Nandi V., Waterson D., Shandil R.,
RA Balganesh M., Sambandamurthy V.K., Raichurkar A.K., Deshpande A., Ghosh A.,
RA Awasthy D., Shanbhag G., Sheikh G., McMiken H., Puttur J., Reddy J.,
RA Werngren J., Read J., Kumar M., R M., Chinnapattu M., Madhavapeddi P.,
RA Manjrekar P., Basu R., Gaonkar S., Sharma S., Hoffner S., Humnabadkar V.,
RA Subbulakshmi V., Panduga V.;
RT "Optimization of pyrrolamides as mycobacterial GyrB ATPase inhibitors:
RT structure-activity relationship and in vivo efficacy in a mouse model of
RT tuberculosis.";
RL Antimicrob. Agents Chemother. 58:61-70(2014).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 448-675, FUNCTION, DOMAIN, AND
RP MUTAGENESIS OF ASP-577; 620-GLU--ASP-627; GLU-620; GLU-623 AND ASP-627.
RX PubMed=19596812; DOI=10.1093/nar/gkp586;
RA Fu G., Wu J., Liu W., Zhu D., Hu Y., Deng J., Zhang X.E., Bi L., Wang D.C.;
RT "Crystal structure of DNA gyrase B' domain sheds lights on the mechanism
RT for T-segment navigation.";
RL Nucleic Acids Res. 37:5908-5916(2009).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 448-675, FUNCTION, AND DOMAIN.
RX PubMed=20805881; DOI=10.1371/journal.pone.0012245;
RA Piton J., Petrella S., Delarue M., Andre-Leroux G., Jarlier V., Aubry A.,
RA Mayer C.;
RT "Structural insights into the quinolone resistance mechanism of
RT Mycobacterium tuberculosis DNA gyrase.";
RL PLoS ONE 5:E12245-E12245(2010).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 2-427 IN COMPLEX WITH ATP ANALOGS
RP AND MAGNESIUM, FUNCTION, AND ATP-BINDING.
RC STRAIN=H37Rv;
RX PubMed=24015710; DOI=10.1042/bj20130538;
RA Agrawal A., Roue M., Spitzfaden C., Petrella S., Aubry A., Hann M., Bax B.,
RA Mayer C.;
RT "Mycobacterium tuberculosis DNA gyrase ATPase domain structures suggest a
RT dissociative mechanism that explains how ATP hydrolysis is coupled to
RT domain motion.";
RL Biochem. J. 456:263-273(2013).
CC -!- FUNCTION: A type II topoisomerase that negatively supercoils closed
CC circular double-stranded (ds) DNA in an ATP-dependent manner to
CC maintain chromosomes in an underwound state, while in the absence of
CC ATP it relaxes supercoiled dsDNA (PubMed:15047530. PubMed:16876125,
CC PubMed:19060136, PubMed:16377674, PubMed:18426901, PubMed:22844097,
CC PubMed:19596812, PubMed:20805881). Also catalyzes the interconversion
CC of other topological isomers of dsDNA rings, including catenanes
CC (PubMed:16876125, PubMed:19060136, PubMed:22457352). Gyrase from
CC M.tuberculosis has higher decatenation than supercoiling activity
CC compared to E.coli; as M.tuberculosis only has 1 type II topoisomerase,
CC gyrase has to fulfill the decatenation function of topoisomerase IV as
CC well (PubMed:16876125, PubMed:22457352, PubMed:23869946). At comparable
CC concentrations M.tuberculosis gyrase cannot introduce as many negative
CC supercoils into DNA as the E.coli enzyme, and its ATPase activity is
CC lower, perhaps because it does not couple DNA wrapping and ATP binding
CC as well as E.coli (PubMed:22457352, PubMed:24015710).
CC {ECO:0000269|PubMed:15047530, ECO:0000269|PubMed:16377674,
CC ECO:0000269|PubMed:16876125, ECO:0000269|PubMed:18426901,
CC ECO:0000269|PubMed:19060136, ECO:0000269|PubMed:19596812,
CC ECO:0000269|PubMed:20805881, ECO:0000269|PubMed:22457352,
CC ECO:0000269|PubMed:22844097, ECO:0000269|PubMed:23869946,
CC ECO:0000269|PubMed:24015710}.
CC -!- FUNCTION: Negative supercoiling favors strand separation, and DNA
CC replication, transcription, recombination and repair, all of which
CC involve strand separation. Type II topoisomerases break and join 2 DNA
CC strands simultaneously in an ATP-dependent manner.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01898,
CC ECO:0000269|PubMed:15047530, ECO:0000269|PubMed:16876125};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01898,
CC ECO:0000269|PubMed:16876125, ECO:0000269|PubMed:24015710};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01898};
CC Note=Mg(2+) required for DNA supercoiling, DNA relaxation, DNA cleavage
CC and DNA decatenation, Mn(2+) substitutes for relaxation but not
CC supercoiling or cleavage activity (PubMed:16876125). Ca(2+) does not
CC substitute for supercoiling activity (PubMed:22844097).
CC {ECO:0000269|PubMed:16876125, ECO:0000269|PubMed:22844097};
CC -!- ACTIVITY REGULATION: DNA supercoiling inhibited by (fluoro)quinoline
CC antibiotics such as sparfloxacin and levofloxacin, which usually act on
CC GyrA subunit (PubMed:15047530). DNA supercoiling inhibited by the
CC coumarin antibiotic novobiocin which acts on GyrB (PubMed:16876125).
CC Quinolones lead to gyrase-mediated dsDNA cleavage while preventing
CC reclosure (PubMed:15047530, PubMed:16876125, PubMed:23869946). DNA
CC supercoiling activity inhibited by aminopyrazinamide and pyrrolamide
CC derivatives, probably via effects on the GyrB subunit (PubMed:23268609,
CC PubMed:24126580). DNA relaxation inhibited by ATP and its analogs
CC (PubMed:16876125). DNA supercoiling, relaxation, decatenation and
CC quinolone-promoted DNA cleavage are inhibited by MfpA (50% inhibition
CC occurs at 2 uM), inhibition of gyrase activities is enhanced in a
CC concentration-dependent manner by MfpA (PubMed:19060136).
CC {ECO:0000269|PubMed:15047530, ECO:0000269|PubMed:16876125,
CC ECO:0000269|PubMed:19060136, ECO:0000269|PubMed:23268609,
CC ECO:0000269|PubMed:23869946, ECO:0000269|PubMed:24126580}.
CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains
CC (PubMed:15047530). In the heterotetramer, GyrA contains the active site
CC tyrosine that forms a transient covalent intermediate with DNA, while
CC GyrB binds cofactors and catalyzes ATP hydrolysis. {ECO:0000255|HAMAP-
CC Rule:MF_01898, ECO:0000269|PubMed:15047530}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01898}.
CC -!- DOMAIN: The B' domain (residues 448-675, Toprim plus a tail domain)
CC forms a dimer; when reconstituted with intact GyrA the complex has ATP-
CC independent DNA relaxation activity (PubMed:19596812). The same
CC fragment (also called TopBK) when reconstituted with intact GyrA or the
CC N-terminus of GyrA (residues 1-502) can catalyze quinolone-mediated DNA
CC breaks (PubMed:20805881). {ECO:0000269|PubMed:19596812,
CC ECO:0000269|PubMed:20805881}.
CC -!- MISCELLANEOUS: When the enzyme transiently cleaves DNA a
CC phosphotyrosine bond is formed between GyrA and DNA (PubMed:15047530).
CC In the presence of quinolones this intermediate can be trapped and is
CC used as an indicator of drug toxicity (PubMed:16377674,
CC PubMed:16876125, PubMed:23869946). DNA gyrase is intrinsically more
CC resistant to fluoroquinolone drugs than in E.coli, mutating it to
CC resemble E.coli increases its susceptibility to fluoroquinolones (most
CC quinolone-resistant mutations are in the GyrA subunit)
CC (PubMed:18426901). {ECO:0000269|PubMed:18426901,
CC ECO:0000305|PubMed:15047530, ECO:0000305|PubMed:16377674,
CC ECO:0000305|PubMed:16876125, ECO:0000305|PubMed:23869946}.
CC -!- MISCELLANEOUS: Gyrase from M.tuberculosis is usually assayed in the
CC presence of potassium glutamate (KGlu); KGlu stimulates supercoiling
CC but inhibits DNA relaxation activity, and has concentration-dependent
CC effects on GyrA-box mutants (PubMed:16876125, PubMed:23869946).
CC {ECO:0000269|PubMed:16876125, ECO:0000269|PubMed:23869946}.
CC -!- MISCELLANEOUS: Few gyrases are as efficient as E.coli at forming
CC negative supercoils. Not all organisms have 2 type II topoisomerases;
CC in organisms with a single type II topoisomerase this enzyme also has
CC to decatenate newly replicated chromosomes. {ECO:0000255|HAMAP-
CC Rule:MF_01898}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC {ECO:0000255|HAMAP-Rule:MF_01898}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA83016.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L27512; AAA83016.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL123456; CCP42727.1; -; Genomic_DNA.
DR PIR; S44198; S44198.
DR RefSeq; NP_214519.2; NC_000962.3.
DR RefSeq; WP_003917863.1; NZ_NVQJ01000005.1.
DR PDB; 2ZJT; X-ray; 2.80 A; A/B=448-675.
DR PDB; 3IG0; X-ray; 2.10 A; A=448-675.
DR PDB; 3M4I; X-ray; 1.95 A; A=448-675.
DR 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.
DR PDB; 3ZKD; X-ray; 2.95 A; A/B/C/D/E/F/G/H=2-427.
DR PDB; 3ZM7; X-ray; 3.30 A; A/B/C/D/E/F=2-428.
DR PDB; 5BS8; X-ray; 2.40 A; B/D=426-675.
DR PDB; 5BTA; X-ray; 2.55 A; B/D=426-675.
DR PDB; 5BTC; X-ray; 2.55 A; B/D=426-675.
DR PDB; 5BTD; X-ray; 2.50 A; B/D=426-675.
DR PDB; 5BTF; X-ray; 2.61 A; B/D=426-675.
DR PDB; 5BTG; X-ray; 2.50 A; B/D=426-675.
DR PDB; 5BTI; X-ray; 2.50 A; B/D=426-675.
DR PDB; 5BTL; X-ray; 2.50 A; B/D=426-675.
DR PDB; 5BTN; X-ray; 2.50 A; B/D=426-675.
DR PDBsum; 2ZJT; -.
DR PDBsum; 3IG0; -.
DR PDBsum; 3M4I; -.
DR PDBsum; 3ZKB; -.
DR PDBsum; 3ZKD; -.
DR PDBsum; 3ZM7; -.
DR PDBsum; 5BS8; -.
DR PDBsum; 5BTA; -.
DR PDBsum; 5BTC; -.
DR PDBsum; 5BTD; -.
DR PDBsum; 5BTF; -.
DR PDBsum; 5BTG; -.
DR PDBsum; 5BTI; -.
DR PDBsum; 5BTL; -.
DR PDBsum; 5BTN; -.
DR AlphaFoldDB; P9WG45; -.
DR SMR; P9WG45; -.
DR STRING; 83332.Rv0005; -.
DR BindingDB; P9WG45; -.
DR ChEMBL; CHEMBL3430898; -.
DR PaxDb; P9WG45; -.
DR DNASU; 887081; -.
DR GeneID; 45423962; -.
DR GeneID; 887081; -.
DR KEGG; mtu:Rv0005; -.
DR TubercuList; Rv0005; -.
DR eggNOG; COG0187; Bacteria.
DR OMA; LWETTMH; -.
DR BRENDA; 5.6.2.2; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IDA:MTBBASE.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0034335; F:DNA negative supercoiling activity; IDA:UniProtKB.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IDA:MTBBASE.
DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR GO; GO:0006265; P:DNA topological change; IBA:GO_Central.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR CDD; cd03366; TOPRIM_TopoIIA_GyrB; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR HAMAP; MF_01898; GyrB; 1.
DR InterPro; IPR002288; DNA_gyrase_B_C.
DR InterPro; IPR011557; GyrB.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR001241; Topo_IIA.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR013759; Topo_IIA_B_C.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034160; TOPRIM_GyrB.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF00986; DNA_gyraseB_C; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00433; TOP2c; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR SUPFAM; SSF56719; SSF56719; 1.
DR TIGRFAMs; TIGR01059; gyrB; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; ATP-binding; Cytoplasm; DNA-binding;
KW Isomerase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Topoisomerase.
FT CHAIN 1..675
FT /note="DNA gyrase subunit B"
FT /id="PRO_0000145325"
FT DOMAIN 453..567
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT BINDING 12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:24015710"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:24015710"
FT BINDING 79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:24015710"
FT BINDING 83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:24015710"
FT BINDING 107..108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:24015710"
FT BINDING 114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:24015710"
FT BINDING 120..125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:24015710"
FT BINDING 169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:24015710"
FT BINDING 370..372
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:24015710"
FT BINDING 459
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT BINDING 532
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT BINDING 532
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT BINDING 534
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT SITE 484
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT SITE 487
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT MUTAGEN 157
FT /note="G->S: Increased resistance to aminopyrazinamides,
FT however genome not sequenced."
FT /evidence="ECO:0000269|PubMed:23268609"
FT MUTAGEN 169
FT /note="S->A: Increased resistance to pyrrolamides and
FT novobiocin, however genome not sequenced."
FT /evidence="ECO:0000269|PubMed:24126580"
FT MUTAGEN 472
FT /note="D->H: No supercoiling activity."
FT /evidence="ECO:0000269|PubMed:16377674"
FT MUTAGEN 482
FT /note="R->K: Increased susceptibility to fluoroquinolones,
FT half supercoiling activity, no fluoroquinolone-induced DNA
FT cleavage (makes sequence more like E.coli)."
FT /evidence="ECO:0000269|PubMed:18426901"
FT MUTAGEN 499
FT /note="N->D: 17-fold increased resistance to
FT fluoroquinolones, slightly increased DNA cleavage in
FT absence of drugs."
FT /evidence="ECO:0000269|PubMed:16377674"
FT MUTAGEN 577
FT /note="D->A: 37% supercoiling, 54% decatenation, 126% DNA
FT cleavage in presence of norfloxacin."
FT /evidence="ECO:0000269|PubMed:19596812"
FT MUTAGEN 577
FT /note="D->R: <2% supercoiling, 4% decatenation."
FT /evidence="ECO:0000269|PubMed:19596812"
FT MUTAGEN 620..627
FT /note="ELWETTMD->ALWETTMA: <3% supercoiling, 18%
FT decatenation, 75% DNA cleavage in presence of norfloxacin."
FT /evidence="ECO:0000269|PubMed:19596812"
FT MUTAGEN 620
FT /note="E->A: 15% supercoiling, 19% decatenation, 143% DNA
FT cleavage in presence of norfloxacin."
FT /evidence="ECO:0000269|PubMed:19596812"
FT MUTAGEN 620
FT /note="E->R: 10% supercoiling, 7% decatenation."
FT /evidence="ECO:0000269|PubMed:19596812"
FT MUTAGEN 623
FT /note="E->A: 18% supercoiling, 11% decatenation, 131% DNA
FT cleavage in presence of norfloxacin."
FT /evidence="ECO:0000269|PubMed:19596812"
FT MUTAGEN 623
FT /note="E->R: <2% supercoiling, 2% decatenation."
FT /evidence="ECO:0000269|PubMed:19596812"
FT MUTAGEN 627
FT /note="D->A: 13% supercoiling, 10% decatenation, 42% DNA
FT cleavage in presence of norfloxacin."
FT /evidence="ECO:0000269|PubMed:19596812"
FT MUTAGEN 627
FT /note="D->R: <2% supercoiling, 3% decatenation."
FT /evidence="ECO:0000269|PubMed:19596812"
FT CONFLICT 291..292
FT /note="MQ -> IE (in Ref. 1; AAA83016)"
FT /evidence="ECO:0000305"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:3ZKB"
FT HELIX 24..28
FT /evidence="ECO:0007829|PDB:3ZKB"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:3ZKB"
FT HELIX 39..58
FT /evidence="ECO:0007829|PDB:3ZKB"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:3ZKB"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:3ZKB"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:3ZKB"
FT HELIX 95..101
FT /evidence="ECO:0007829|PDB:3ZKB"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:3ZKB"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:3ZKB"
FT HELIX 124..130
FT /evidence="ECO:0007829|PDB:3ZKB"
FT STRAND 132..141
FT /evidence="ECO:0007829|PDB:3ZKB"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:3ZKB"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:3ZKB"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:3ZKB"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:3ZKB"
FT HELIX 187..199
FT /evidence="ECO:0007829|PDB:3ZKB"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:3ZKB"
FT HELIX 236..241
FT /evidence="ECO:0007829|PDB:3ZKD"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:3ZKB"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:3ZKB"
FT HELIX 257..264
FT /evidence="ECO:0007829|PDB:3ZKB"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:3ZKB"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:3ZKD"
FT STRAND 276..282
FT /evidence="ECO:0007829|PDB:3ZKB"
FT STRAND 285..298
FT /evidence="ECO:0007829|PDB:3ZKB"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:3ZKB"
FT HELIX 315..334
FT /evidence="ECO:0007829|PDB:3ZKB"
FT HELIX 347..351
FT /evidence="ECO:0007829|PDB:3ZKB"
FT STRAND 354..360
FT /evidence="ECO:0007829|PDB:3ZKB"
FT TURN 369..372
FT /evidence="ECO:0007829|PDB:3ZKB"
FT HELIX 378..398
FT /evidence="ECO:0007829|PDB:3ZKB"
FT HELIX 400..422
FT /evidence="ECO:0007829|PDB:3ZKB"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:3M4I"
FT STRAND 453..462
FT /evidence="ECO:0007829|PDB:3M4I"
FT STRAND 475..481
FT /evidence="ECO:0007829|PDB:3M4I"
FT TURN 488..490
FT /evidence="ECO:0007829|PDB:5BS8"
FT HELIX 493..496
FT /evidence="ECO:0007829|PDB:3M4I"
FT HELIX 500..509
FT /evidence="ECO:0007829|PDB:3M4I"
FT HELIX 514..516
FT /evidence="ECO:0007829|PDB:3M4I"
FT HELIX 519..521
FT /evidence="ECO:0007829|PDB:3M4I"
FT STRAND 525..530
FT /evidence="ECO:0007829|PDB:3M4I"
FT HELIX 535..551
FT /evidence="ECO:0007829|PDB:3M4I"
FT HELIX 554..557
FT /evidence="ECO:0007829|PDB:3M4I"
FT STRAND 561..564
FT /evidence="ECO:0007829|PDB:3M4I"
FT STRAND 568..571
FT /evidence="ECO:0007829|PDB:3M4I"
FT STRAND 573..576
FT /evidence="ECO:0007829|PDB:5BS8"
FT STRAND 579..583
FT /evidence="ECO:0007829|PDB:3M4I"
FT HELIX 584..597
FT /evidence="ECO:0007829|PDB:3M4I"
FT TURN 603..605
FT /evidence="ECO:0007829|PDB:3M4I"
FT STRAND 606..609
FT /evidence="ECO:0007829|PDB:3M4I"
FT HELIX 613..615
FT /evidence="ECO:0007829|PDB:3M4I"
FT HELIX 618..625
FT /evidence="ECO:0007829|PDB:3M4I"
FT TURN 628..630
FT /evidence="ECO:0007829|PDB:3M4I"
FT STRAND 633..635
FT /evidence="ECO:0007829|PDB:3M4I"
FT HELIX 638..653
FT /evidence="ECO:0007829|PDB:3M4I"
FT HELIX 656..666
FT /evidence="ECO:0007829|PDB:5BS8"
FT HELIX 667..672
FT /evidence="ECO:0007829|PDB:5BS8"
SQ 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
