GYRB_BORBU
ID GYRB_BORBU Reviewed; 634 AA.
AC P33769; O30779;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 4.
DT 03-AUG-2022, entry version 142.
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};
GN Name=gyrB {ECO:0000255|HAMAP-Rule:MF_01898}; OrderedLocusNames=BB_0436;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=8188609; DOI=10.1128/jb.176.10.3072-3075.1994;
RA Samuels D.S., Marconi R.T., Huang W.M., Garon C.F.;
RT "gyrB mutations in coumermycin A1-resistant Borrelia burgdorferi.";
RL J. Bacteriol. 176:3072-3075(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-380.
RC STRAIN=212;
RX PubMed=8359672; DOI=10.1111/j.1574-6968.1993.tb06369.x;
RA Old I.G., Margarita D., Saint-Girons I.;
RT "Unique genetic arrangement in the dnaA region of the Borrelia burgdorferi
RT linear chromosome: nucleotide sequence of the dnaA gene.";
RL FEMS Microbiol. Lett. 111:109-114(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 297-380.
RC STRAIN=212;
RX PubMed=1490605; DOI=10.1016/0378-1097(92)90034-l;
RA Old I.G., Macdougall J.H., Saint-Girons I., Davidson B.E.;
RT "Mapping of genes on the linear chromosome of the bacterium Borrelia
RT burgdorferi: possible locations for its origin of replication.";
RL FEMS Microbiol. Lett. 78:245-250(1992).
CC -!- FUNCTION: A type II topoisomerase that negatively supercoils closed
CC circular double-stranded (ds) DNA in an ATP-dependent manner to
CC modulate DNA topology and maintain chromosomes in an underwound state.
CC Negative supercoiling favors strand separation, and DNA replication,
CC transcription, recombination and repair, all of which involve strand
CC separation. Also able to catalyze the interconversion of other
CC topological isomers of dsDNA rings, including catenanes and knotted
CC rings. Type II topoisomerases break and join 2 DNA strands
CC simultaneously in an ATP-dependent manner. {ECO:0000255|HAMAP-
CC Rule:MF_01898}.
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-
CC Rule:MF_01898};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01898};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01898};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01898};
CC Note=Binds two Mg(2+) per subunit. The magnesium ions form salt bridges
CC with both the protein and the DNA. Can also accept other divalent metal
CC cations, such as Mn(2+) or Ca(2+). {ECO:0000255|HAMAP-Rule:MF_01898};
CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains. In
CC the heterotetramer, GyrA contains the active site tyrosine that forms a
CC transient covalent intermediate with DNA, while GyrB binds cofactors
CC and catalyzes ATP hydrolysis. {ECO:0000255|HAMAP-Rule:MF_01898}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01898}.
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=AAA58940.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF017075; AAB67237.1; -; Genomic_DNA.
DR EMBL; AE000783; AAC66802.2; -; Genomic_DNA.
DR EMBL; U04527; AAA58940.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z12166; CAA78158.1; -; Genomic_DNA.
DR PIR; C70154; C70154.
DR RefSeq; NP_212570.2; NC_001318.1.
DR RefSeq; WP_010889750.1; NC_001318.1.
DR AlphaFoldDB; P33769; -.
DR SMR; P33769; -.
DR STRING; 224326.BB_0436; -.
DR PRIDE; P33769; -.
DR EnsemblBacteria; AAC66802; AAC66802; BB_0436.
DR KEGG; bbu:BB_0436; -.
DR PATRIC; fig|224326.49.peg.827; -.
DR HOGENOM; CLU_006146_1_2_12; -.
DR Proteomes; UP000001807; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA-binding; Isomerase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Topoisomerase.
FT CHAIN 1..634
FT /note="DNA gyrase subunit B"
FT /id="PRO_0000145296"
FT DOMAIN 416..530
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT BINDING 422
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 495
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 495
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT BINDING 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT SITE 447
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT SITE 450
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT CONFLICT 51
FT /note="G -> A (in Ref. 3; AAA58940)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="A -> VT (in Ref. 3; AAA58940)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 634 AA; 71451 MW; 69D5FFDBC0957C55 CRC64;
MNYVASNIQV LKGLEAVRKR PGMYIGSVSI NGLHHLVYEV VDNSIDEALA GFCDRIDVII
NLDNTITVID NGRGIPTDIH EEEGISALEL VLTKLHSGGK FNKGTYKVSG GLHGVGISVV
NALSSFLEVY VNRDGKIFRQ TFSKGIPTSK VEVVGESSVT GTKVTFLADS EIFETLDYNF
DVLEKRLKEL AFLNDKIYIS IEDKRIGKEK SSKFYFEGGI KSFVDYLTND SKAFQSEPYY
IDGFINDVIV NVGLKWTESY SDNILSFVNN INTREGGTHV MGFRSGLTKA MNEAFKNSKI
SKKDIPNLTG DDFKEGLTAV ISVKVPEPQF EGQTKSKLGN SEIRKIVEVV VYEHLLEIIN
LNPLEIDTIL GKAIKAARAR EAARKARESE RKKNAFESLA LPGKLADCTS KNPLEREIYI
VEGDSAGGSA KMGRNRFFQA ILPLWGKMLN VEKTREDKVI TNDKLIPIIA SLGAGVGKTF
DITKLRYHKI IIMADADVDG SHIRTLLLAF FFRYMRDLIE NGYIYIAMPP LYKIKYDNRI
YYFYEEKEKE KFLDSIETKN RNSISLQRYK GLGEMNPTQL WETTMDPARR KMRLMNIDDA
IEAEKIFVTL MGDLVEPRKE FIEQNALNVI NLDV
