ID   GYRB_MYXXA              Reviewed;         815 AA.
AC   O33367;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 101.
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};
OS   Myxococcus xanthus.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=34;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ER-15;
RX   PubMed=9639935; DOI=10.1099/00221287-144-6-1641;
RA   Paitan Y., Boulton N., Ron E.Z., Rosenberg E., Orr E.;
RT   "Molecular analysis of the DNA gyrB gene from Myxococcus xanthus.";
RL   Microbiology 144:1641-1647(1998).
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}.
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DR   EMBL; AJ000543; CAA04176.1; -; Genomic_DNA.
DR   AlphaFoldDB; O33367; -.
DR   SMR; O33367; -.
DR   PRIDE; O33367; -.
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   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   Gene3D; 3.40.50.670; -; 2.
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   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   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; Topoisomerase.
FT   CHAIN           1..815
FT                   /note="DNA gyrase subunit B"
FT                   /id="PRO_0000145326"
FT   DOMAIN          430..545
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         436
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         509
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         509
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT   BINDING         511
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT   SITE            461
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT   SITE            464
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
SQ   SEQUENCE   815 AA;  89637 MW;  3862685FBB805B32 CRC64;
     MEKTPATGSA VAPPPVEYGT DSITKLEGRE AVRKRPGMYI GDTMAYGLHK LVYEVVDNAV
     DESLAGHCTD IEVVIHVDGS LSVQDNGRGI PVGPHPKFPG KDTLEVVLTE LHAGSKFGNG
     AYKVSGGLHG VGVTCVNFLS EWFKVRVHRN GIVYEQAYAQ GVPDTPPREV GTTDKRGTHI
     AFKPDATVME LVEFNFETLS QRLRELAFLN AGLHIVVRDE RTNKEHDFKF DGGISSFVEY
     LNKSKQTLHD KPISFSTERE GVMLDIAMQW NDGYDERIYT FANNINTHEG GSHLSGFKAA
     LTRTLNSYAE KGSLWKDLKE TPTGEDAREG LSAVISVKLT NPQFEGQTKT KLGNSEVKGL
     VEQMVNDQLG SFLEETPMVA KKVVAKIGDA CRARLAARKA RETVRRKGVL DGGGLPGKLA
     DCQIRDPNES ELYIVEGDSA GGSAKQGRDR RNQAILPLRG KILNVEKLLR EMLTSAEIVT
     LITALGNGIG AEDYDPEKAR YHRIFLMTDA DVDGSHIRTL LLTSSSGRCR SSCRRAISTS
     RSRRSYKVTR NKKDQYVKDE HALNEYLLKI ASEHARVLTP GGELGGAELK ALLEKVITYE
     ERLEKQAKRR DARVVDALVQ GARLSAETLT GRGCPGGGGE GRLMTPSSAA CRTCWAACAT
     SWCRTPSTTP RSWCSTPTRM EPCGRRCSTT PSCRRRSTWS CRLCAEHLRG AGQGAVQGPR
     GRGEITVFSV QEVLAAVRKD AQRGLGLQRY KGLGEMNPEQ LWDTTMNPAT RTLLQVRVED
     AVESDEIFSL LMGEAVEPRR EFIERNALDV QNLDI