ID A0A0A7ECG3_9GAMM Unreviewed; 805 AA. AC A0A0A7ECG3; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 20-JAN-2016, entry version 10. DE RecName: Full=DNA gyrase subunit B {ECO:0000256|HAMAP-Rule:MF_01898, ECO:0000256|SAAS:SAAS00363408}; 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: 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}. 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 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}. 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: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|SAAS:SAAS00106864}; Coiled coil {ECO:0000256|SAM:Coils}; 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:SAAS00107007}; 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|SAAS:SAAS00106998}; KW Reference proteome {ECO:0000313|Proteomes:UP000030341}; KW Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01898, KW ECO:0000256|SAAS:SAAS00107032}. FT DOMAIN 419 534 Toprim. {ECO:0000256|HAMAP-Rule:MF_01898, FT ECO:0000259|PROSITE:PS50880}. FT COILED 581 601 {ECO:0000256|SAM:Coils}. 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 //