ID A0A0A7ECG3_9GAMM Unreviewed; 805 AA. AC A0A0A7ECG3; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 11-MAY-2016, entry version 13. DE RecName: Full=DNA gyrase subunit B {ECO:0000256|HAMAP-Rule:MF_01898, ECO:0000256|SAAS:SAAS00555050}; 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: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, ECO:0000313|Proteomes:UP000030341} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OCN003 {ECO:0000313|EMBL:AIY64279.1, RC ECO:0000313|Proteomes:UP000030341}; 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: 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; 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 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}. CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000256|HAMAP- CC Rule:MF_01898}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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:UniProtKB-HAMAP. 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|SAAS:SAAS00528655}; 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|SAAS:SAAS00470744}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01898, KW ECO:0000256|SAAS:SAAS00445358}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01898, KW ECO:0000256|SAAS:SAAS00445373}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01898, KW ECO:0000256|SAAS:SAAS00528653}; KW Reference proteome {ECO:0000313|Proteomes:UP000030341}; KW Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01898, KW ECO:0000256|SAAS:SAAS00528650}. FT DOMAIN 419 534 Toprim. {ECO:0000259|PROSITE:PS50880}. 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 //