(data stored in ACNUC7421 zone)

SWISSPROT: D4YWZ9_SPHJU

ID   D4YWZ9_SPHJU            Unreviewed;       835 AA.
AC   D4YWZ9;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 59.
DE   RecName: Full=DNA gyrase subunit B {ECO:0000256|HAMAP-Rule:MF_01898, ECO:0000256|SAAS:SAAS00746468};
DE            EC=5.99.1.3 {ECO:0000256|HAMAP-Rule:MF_01898, ECO:0000256|SAAS:SAAS00470646};
GN   Name=gyrB {ECO:0000256|HAMAP-Rule:MF_01898,
GN   ECO:0000313|EMBL:BAI94881.1};
GN   OrderedLocusNames=SJA_C1-00470 {ECO:0000313|EMBL:BAI94881.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI94881.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI94881.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
CC   -!- FUNCTION: A type II topoisomerase that negatively supercoils
CC       closed circular double-stranded (ds) DNA in an ATP-dependent
CC       manner to modulate DNA topology and maintain chromosomes in an
CC       underwound state. Negative supercoiling favors strand separation,
CC       and DNA replication, transcription, recombination and repair, all
CC       of which involve strand separation. Also able to catalyze the
CC       interconversion of other topological isomers of dsDNA rings,
CC       including catenanes and knotted rings. Type II topoisomerases
CC       break and join 2 DNA strands simultaneously in an ATP-dependent
CC       manner. {ECO:0000256|HAMAP-Rule:MF_01898}.
CC   -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining
CC       of double-stranded DNA. {ECO:0000256|HAMAP-Rule:MF_01898,
CC       ECO:0000256|SAAS:SAAS00470725}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00609977};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00709652};
CC   -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains.
CC       In the heterotetramer, GyrA contains the active site tyrosine that
CC       forms a transient covalent intermediate with DNA, while GyrB binds
CC       cofactors and catalyzes ATP hydrolysis. {ECO:0000256|HAMAP-
CC       Rule:MF_01898}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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
CC       topoisomerases; in organisms with a single type II topoisomerase
CC       this enzyme also has to decatenate newly replicated chromosomes.
CC       {ECO:0000256|HAMAP-Rule:MF_01898}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01898}.
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DR   EMBL; AP010803; BAI94881.1; -; Genomic_DNA.
DR   RefSeq; WP_013038723.1; NC_014006.1.
DR   ProteinModelPortal; D4YWZ9; -.
DR   STRING; 452662.SJA_C1-00470; -.
DR   EnsemblBacteria; BAI94881; BAI94881; SJA_C1-00470.
DR   GeneID; 29271757; -.
DR   KEGG; sjp:SJA_C1-00470; -.
DR   eggNOG; ENOG4105C7D; Bacteria.
DR   eggNOG; COG0187; LUCA.
DR   HOGENOM; HOG000075155; -.
DR   KO; K02470; -.
DR   OMA; DCSSRDP; -.
DR   OrthoDB; POG091H01XP; -.
DR   Proteomes; UP000007753; Chromosome 1.
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-HAMAP.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-HAMAP.
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; 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.
DR   InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR   InterPro; IPR013759; Topo_IIA_cen_dom.
DR   InterPro; IPR018522; TopoIIA_CS.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034160; TOPRIM_GyrB.
DR   PANTHER; PTHR10169; PTHR10169; 1.
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   PRINTS; PR00418; TPI2FAMILY.
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; 2.
DR   TIGRFAMs; TIGR01059; gyrB; 1.
DR   PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
DR   PRODOM; D4YWZ9.
DR   SWISS-2DPAGE; D4YWZ9.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00528655};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01898};
KW   DNA-binding {ECO:0000256|SAAS:SAAS00709661};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00107007, ECO:0000313|EMBL:BAI94881.1};
KW   Magnesium {ECO:0000256|SAAS:SAAS00058309};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00058330};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00528653};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00528650}.
FT   DOMAIN      442    556       Toprim. {ECO:0000259|PROSITE:PS50880}.
SQ   SEQUENCE   835 AA;  92425 MW;  1BF72E649523EF0A CRC64;
     MSEESQNNPN SNAYGADSIK VLKGLDAVRK RPGMYIGDTD DGSGLHHMVF EVSDNAIDEA
     LAGHCDRILI TLNPDGSVSV EDNGRGIPTD IHKEEGVSAA EVIMTQLHAG GKFENTSDDN
     AYKVSGGLHG VGVSVVNALS EYLDLNIWRD GKEHYMRFAY GDAVAPLKVI GDAPEGKKGT
     KVTFLPSTEK VPGDGGTFKN HTEFDFEKLE HRYRELAFLN SGVRLFLADA RHEEKKEIEL
     FYEGGIAAFV KWLDRNKQPL MPDPIAISGS RDDVTIDVAL EWNDSYYENV LCFTNNIPQR
     DGGTHLAAFR AALTRTLNNY ADKSGLLKKE KVSLTGEDMR EGLTAIVSVK LPDPKFSSQT
     KDKLVSSEVR QPLESLMADK MAEWLEENPQ HGRMIVQKVI DAAAAREAAK KARELTRRKG
     VMDIASLPGK LADCQERDPA KSELFLVEGD SAGGSAKQGR NRHNQAILPL KGKILNVERA
     RFDRMLSSKE VGTLIQAMGT GIRDDFNLEK LRYHKIVIMT DADVDGAHIR TLLLTFFYRQ
     MPQIIEAGHL YIAQPPLYKA TRGRSEVYLK NEAALENYLV DNGVESMALE TTGGMRSGED
     LRSLIEHGRR IRAVMRYVPR RYNPAIIEAL AINGALDPEL SHDAQAERLA NTVRWMDAQD
     DEGRWSGRIA EEGGFHFERL WRGVTDHHMI EAGFIGSAEA RKLHAIAAEE ADSYRTSSRL
     VTAKAAAAAE EAGEDELPVA TKGSATVTRP SELLEAILTA GRKGLAIQRY KGLGEMNAEQ
     LWETTLDPDN RSMLRVEVEQ ADVADEIFTR LMGDVVEPRR EFIQDNALNV ANLDV
//

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