ID   A0A0A7ECG3_9GAMM        Unreviewed;       805 AA.
AC   A0A0A7ECG3;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   16-SEP-2015, entry version 6.
DE   RecName: Full=DNA gyrase subunit B {ECO:0000256|HAMAP-Rule:MF_01898, ECO:0000256|RuleBase:RU003363};
DE            EC=5.99.1.3 {ECO:0000256|HAMAP-Rule:MF_01898, ECO:0000256|RuleBase:RU003363};
GN   Name=gyrB {ECO:0000256|HAMAP-Rule:MF_01898,
GN   ECO:0000313|EMBL:AIY64279.1};
GN   ORFNames=OM33_03245 {ECO:0000313|EMBL:AIY64279.1};
OS   Pseudoalteromonas sp. OCN003.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1348114 {ECO:0000313|EMBL:AIY64279.1, ECO:0000313|Proteomes:UP000030341};
RN   [1] {ECO:0000313|EMBL:AIY64279.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OCN003 {ECO:0000313|EMBL:AIY64279.1};
RA   Beurmann S., Videau P., Ushijima B., Smith A.M., Aeby G.S.,
RA   Callahan S.M., Belcaid M.;
RT   "Complete Genome Sequence of Pseudoalteromonas sp. Strain OCN003
RT   Isolated from Kaneohe Bay, Oahu, Hawaii.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA gyrase negatively supercoils closed circular double-
CC       stranded DNA in an ATP-dependent manner and also catalyzes the
CC       interconversion of other topological isomers of double-stranded
CC       DNA rings, including catenanes and knotted rings.
CC       {ECO:0000256|HAMAP-Rule:MF_01898, ECO:0000256|RuleBase:RU003363}.
CC   -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining
CC       of double-stranded DNA. {ECO:0000256|HAMAP-Rule:MF_01898,
CC       ECO:0000256|RuleBase:RU003363, ECO:0000256|SAAS:SAAS00048791}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01898};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01898};
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01898};
CC       Note=Binds two Mg(2+) per subunit. The magnesium ions form salt
CC       bridges with both the protein and the DNA. Can also accept other
CC       divalent metal cations, such as Mn(2+) or Ca(2+).
CC       {ECO:0000256|HAMAP-Rule:MF_01898};
CC   -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains.
CC       Within the heterotetramer, GyrA contains the active site tyrosine
CC       that forms a covalent intermediate with the DNA, while GyrB
CC       contributes the cofactor binding sites and catalyzes ATP
CC       hydrolysis. {ECO:0000256|HAMAP-Rule:MF_01898}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01898}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01898, ECO:0000256|RuleBase:RU000380}.
CC   -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000256|HAMAP-
CC       Rule:MF_01898}.
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DR   EMBL; CP009888; AIY64279.1; -; Genomic_DNA.
DR   RefSeq; WP_038638712.1; NZ_CP009888.1.
DR   EnsemblBacteria; AIY64279; AIY64279; OM33_03245.
DR   KEGG; pseo:OM33_03245; -.
DR   KO; K02470; -.
DR   Proteomes; UP000030341; 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-HAMAP.
DR   GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-HAMAP.
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; 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   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;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|RuleBase:RU000380};
KW   Complete proteome {ECO:0000313|Proteomes:UP000030341};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01898};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01898};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|RuleBase:RU000380};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01898};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01898};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|RuleBase:RU000380};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030341};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|RuleBase:RU000380}.
FT   DOMAIN      419    534       Toprim. {ECO:0000256|HAMAP-Rule:
FT                                MF_01898}.
FT   METAL       425    425       Magnesium 1; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01898}.
FT   METAL       499    499       Magnesium 1; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01898}.
FT   METAL       499    499       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01898}.
FT   METAL       501    501       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01898}.
FT   SITE        450    450       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_01898}.
FT   SITE        453    453       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_01898}.
SQ   SEQUENCE   805 AA;  89794 MW;  401E1512C37E5E89 CRC64;
     MSENYDSSSI KVLKGLDAVR KRPGMYIGDT DDGTGLHHMV FEVVDNSIDE ALAGYCDDVY
     VTIHSDGSVS VRDNGRGIPT EIHEEEGVSA AEVIMTVLHA GGKFDDNSYK VSGGLHGVGV
     SVVNALSEKL KLTIRRGGKI HEQTYNMGEP AAPLAVVGDS ETNGTEIRFW PSAETFSDTN
     FHYDILAKRL RELSFLNSGV SIILSDERDE KRDHFKYEGG IQAFVEFLNT NKTPVNQNVF
     HFTSTREEDG ISVEVAMQWN DGFQEGIYCF TNNIPQRDGG THLAGFRSAL TRTLNTYMDK
     EGFNKKEKSS ASGDDAREGL TAVISVKVPD PKFSSQTKDK LVSSEVKSAV EQAMGEKLSE
     YLLENPQDAK IVVTKIIDAA RAREAARKAR EMTRRKGAMD LAGLPGKLAD CQEKDPALSE
     LYIVEGDSAG GSAKQGRNRK NQAILPLKGK ILNVEKARFD KMLSSQEVAT LITALGCGIG
     RDEYNPEKLR YHSIIIMTDA DVDGSHIRTL LLTFFYRQMP EIVERGYVYI AQPPLYKVKK
     GKQERYIKDD PALTEYLTTL ALDGSSLHVN EEAPGISDVA LEALVKDYQA TEAIITRLTR
     KYPLSVLNSL IYSTRINEAD LADEAKVRTW TESVVAYLTE KDVDATLFTA EVKKDEERNL
     FYPNIVIRQH GVDREHVLNY EFLTSRDYLS IAKTGEQIGN LIEEGGYIQR GEKTLQVSSF
     VEALDWLISE SKRGLYIQRY KGLGEMNPDQ LWETTMDPEV RRMLKVTIED AIGADQLFST
     LMGDQVEPRR DFIEQNALKV VNLDV
//