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DNA gyrase subunit B (EC 5.99.1.3)

 A0A193PPK3_9VIBR        Unreviewed;       812 AA.
A0A193PPK3;
05-OCT-2016, integrated into UniProtKB/TrEMBL.
05-OCT-2016, sequence version 1.
25-OCT-2017, entry version 9.
RecName: Full=DNA gyrase subunit B {ECO:0000256|HAMAP-Rule:MF_01898};
EC=5.99.1.3 {ECO:0000256|HAMAP-Rule:MF_01898};
Name=gyrB {ECO:0000256|HAMAP-Rule:MF_01898,
ECO:0000313|EMBL:BAV18313.1};
Vibrio algivorus.
Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
Vibrionaceae; Vibrio.
NCBI_TaxID=1667024 {ECO:0000313|EMBL:BAV18313.1};
[1] {ECO:0000313|EMBL:BAV18313.1}
NUCLEOTIDE SEQUENCE.
STRAIN=SA2 {ECO:0000313|EMBL:BAV18313.1};
Doi H., Chinen A., Fukuda H., Usuda Y.;
"Vibrio algivorus sp. nov., an alginate and agarose assimilating
bacterium isolated from the gut flora of a turban shell marine
snail.";
Int. J. Syst. Evol. Microbiol. 0:0-0(2016).
-!- FUNCTION: A type II topoisomerase that negatively supercoils
closed circular double-stranded (ds) DNA in an ATP-dependent
manner to modulate DNA topology and maintain chromosomes in an
underwound state. Negative supercoiling favors strand separation,
and DNA replication, transcription, recombination and repair, all
of which involve strand separation. Also able to catalyze the
interconversion of other topological isomers of dsDNA rings,
including catenanes and knotted rings. Type II topoisomerases
break and join 2 DNA strands simultaneously in an ATP-dependent
manner. {ECO:0000256|HAMAP-Rule:MF_01898}.
-!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining
of double-stranded DNA. {ECO:0000256|HAMAP-Rule:MF_01898,
ECO:0000256|SAAS:SAAS00924961}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|SAAS:SAAS00907948};
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000256|SAAS:SAAS00888357};
-!- 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. {ECO:0000256|HAMAP-
Rule:MF_01898}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01898}.
-!- 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:0000256|HAMAP-Rule:MF_01898}.
-!- SIMILARITY: Belongs to the type II topoisomerase family.
{ECO:0000256|HAMAP-Rule:MF_01898}.
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EMBL; LC164152; BAV18313.1; -; Genomic_DNA.
GO; GO:0005694; C:chromosome; IEA:InterPro.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-UniRule.
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.
InterPro; IPR013506; Topo_IIA_bsu_dom2.
InterPro; IPR013759; Topo_IIA_cen_dom.
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; 2.
TIGRFAMs; TIGR01059; gyrB; 1.
PROSITE; PS00177; TOPOISOMERASE_II; 1.
PROSITE; PS50880; TOPRIM; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01898,
ECO:0000256|SAAS:SAAS00924926};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01898};
DNA-binding {ECO:0000256|SAAS:SAAS00888349};
Isomerase {ECO:0000256|HAMAP-Rule:MF_01898,
ECO:0000256|SAAS:SAAS00924964};
Magnesium {ECO:0000256|SAAS:SAAS00906748};
Metal-binding {ECO:0000256|SAAS:SAAS00906804};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01898,
ECO:0000256|SAAS:SAAS00924926};
Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01898,
ECO:0000256|SAAS:SAAS00924964}.
DOMAIN 426 541 Toprim. {ECO:0000259|PROSITE:PS50880}.
SEQUENCE 812 AA; 90635 MW; E51D1D28861B975F CRC64;
MSNNNDSANS YDSSSIKVLK GLDAVRKRPG MYIGDTDDGT GLHHMVFEVV DNSIDEALAG
HCSDIIITIH EDNSVSVSDD GRGIPTEMHE EEGVSAAEVI MTVLHAGGKF DDNSYKVSGG
LHGVGVSVVN ALSEKVELTI KRQGEIFQQV YKHGVPEAPL AVIGKTEETG TRIRFWPSEE
TFTNIEFHYD ILAKRLRELS FLNSGVSIKL TDEREEDKSD HFMFEGGIRA FVEHLNRNKT
PIHQKIFYFD HSREEDGITV EVAMQWNDTF QEGVYCFTNN IPQRDGGTHL AGFRGALTRT
LNNFMDKEGY SKKAQAATSG DDAREGLTAV VSVKVPDPKF SSQTKDKLVS SEVKSAVESA
MSEKLSEFLI ENPNEAKIVC GKIIDAARAR EAARKARDMT RRKGALDLAG LPGKLADCQE
KDPALSELYI VEGDSAGGSA KQGRNRKNQA ILPLKGKILN VEKARFDKML SSQEVATLIT
ALGCGIGRDE YNPDKLRYHN IIIMTDADVD GSHIRTLLLT FFYRQMPELI ERGYIYIAQP
PLYKVKKGKQ EQYIKDEEAM ELYQAGLALD GAALYVNPQA PAMTGEALEK LVLQYNEGIK
LIKRMSRRYP YAMINELTYI PRLTADMCQD SEQVQAWGQK LVEQLNAKEV GASQYSLEVE
KHQELGISIP KLVVRTHGVM HEYVVSLDLL NSKEYGRLAD LSEALDGLVE EGAYVKRGER
TQEVSTFSAA LEWLIKESRR GLSLQRYKGL GEMNPDQLWE TTMDPETRRM MQVTIDDAVA
SDELFTTLMG DQVEPRRKFI EDNALKVANL DV


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