ID A0A0A7ECG3_9GAMM Unreviewed; 805 AA. AC A0A0A7ECG3; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 08-NOV-2023, entry version 47. DE RecName: Full=DNA gyrase subunit B {ECO:0000256|ARBA:ARBA00019166, ECO:0000256|HAMAP-Rule:MF_01898}; DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895, ECO:0000256|HAMAP-Rule:MF_01898}; 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 piratica. OC Bacteria; Pseudomonadota; 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., Callahan S.M., RA Belcaid M.; RT "Complete Genome Sequence of Pseudoalteromonas sp. Strain OCN003 Isolated RT from Kaneohe Bay, Oahu, Hawaii."; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: A type II topoisomerase that negatively supercoils closed CC circular double-stranded (ds) DNA in an ATP-dependent manner to CC modulate DNA topology and maintain chromosomes in an underwound state. CC Negative supercoiling favors strand separation, and DNA replication, CC transcription, recombination and repair, all of which involve strand CC separation. Also able to catalyze the interconversion of other CC topological isomers of dsDNA rings, including catenanes and knotted CC rings. Type II topoisomerases break and join 2 DNA strands CC simultaneously in an ATP-dependent manner. {ECO:0000256|HAMAP- CC Rule:MF_01898}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP-dependent breakage, passage and rejoining of double- CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00000185, CC ECO:0000256|HAMAP-Rule:MF_01898}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01898}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01898}; CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01898}; CC Note=Binds two Mg(2+) per subunit. The magnesium ions form salt bridges CC with both the protein and the DNA. Can also accept other divalent metal CC cations, such as Mn(2+) or Ca(2+). {ECO:0000256|HAMAP-Rule:MF_01898}; CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains. In CC the heterotetramer, GyrA contains the active site tyrosine that forms a CC transient covalent intermediate with DNA, while GyrB binds cofactors CC and catalyzes ATP hydrolysis. {ECO:0000256|HAMAP-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 topoisomerases; CC in organisms with a single type II topoisomerase this enzyme also has CC to decatenate newly replicated chromosomes. {ECO:0000256|HAMAP- CC Rule:MF_01898}. CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family. CC {ECO:0000256|ARBA:ARBA00010708, ECO:0000256|HAMAP-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 AlphaFoldDB; A0A0A7ECG3; -. DR STRING; 1348114.OM33_03245; -. DR EnsemblBacteria; AIY64279; AIY64279; OM33_03245. DR KEGG; pseo:OM33_03245; -. DR eggNOG; COG0187; Bacteria. DR HOGENOM; CLU_006146_4_1_6; -. DR OrthoDB; 9802808at2; -. 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-UniRule. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule. DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule. DR CDD; cd16928; HATPase_GyrB-like; 1. DR CDD; cd00822; TopoII_Trans_DNA_gyrase; 1. DR CDD; cd03366; TOPRIM_TopoIIA_GyrB; 1. DR Gene3D; 3.10.20.690; -; 1. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.40.50.670; -; 2. DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1. DR HAMAP; MF_01898; GyrB; 1. DR InterPro; IPR002288; DNA_gyrase_B_C. DR InterPro; IPR011557; GyrB. DR InterPro; IPR041423; GyrB_insert. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR036890; HATPase_C_sf. DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF. DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr. DR InterPro; IPR001241; Topo_IIA. DR InterPro; IPR013760; Topo_IIA-like_dom_sf. DR InterPro; IPR000565; Topo_IIA_B. DR InterPro; IPR013759; Topo_IIA_B_C. DR InterPro; IPR013506; Topo_IIA_bsu_dom2. DR InterPro; IPR018522; TopoIIA_CS. DR InterPro; IPR006171; TOPRIM_domain. DR InterPro; IPR034160; TOPRIM_GyrB. DR NCBIfam; TIGR01059; gyrB; 1. DR PANTHER; PTHR45866:SF1; DNA GYRASE SUBUNIT B, MITOCHONDRIAL; 1. DR PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1. DR Pfam; PF00204; DNA_gyraseB; 1. DR Pfam; PF00986; DNA_gyraseB_C; 1. DR Pfam; PF18053; GyrB_insert; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF01751; Toprim; 1. DR PRINTS; PR01159; DNAGYRASEB. DR PRINTS; PR00418; TPI2FAMILY. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00433; TOP2c; 1. DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1. DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1. DR PROSITE; PS00177; TOPOISOMERASE_II; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01898}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01898}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01898}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01898}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01898}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01898}; Reference proteome {ECO:0000313|Proteomes:UP000030341}; KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP- KW Rule:MF_01898}. FT DOMAIN 419..534 FT /note="Toprim" FT /evidence="ECO:0000259|PROSITE:PS50880" FT BINDING 425 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01898" FT BINDING 499 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01898" FT BINDING 499 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01898" FT BINDING 501 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01898" FT SITE 450 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01898" FT SITE 453 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-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 //