ID A0A1Z2KZK2_9ACTN Unreviewed; 706 AA.
AC A0A1Z2KZK2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN Name=gyrB {ECO:0000313|EMBL:ARZ67446.1};
GN ORFNames=SMD11_1785 {ECO:0000313|EMBL:ARZ67446.1};
OS Streptomyces albireticuli.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1940 {ECO:0000313|EMBL:ARZ67446.1, ECO:0000313|Proteomes:UP000195755};
RN [1] {ECO:0000313|EMBL:ARZ67446.1, ECO:0000313|Proteomes:UP000195755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MDJK11 {ECO:0000313|EMBL:ARZ67446.1,
RC ECO:0000313|Proteomes:UP000195755};
RA Wang Y., Du B., Ding Y., Liu H., Hou Q., Liu K., Yao L., Wang C.;
RT "Streptomyces albireticuli Genome sequencing and assembly.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC {ECO:0000256|ARBA:ARBA00010708}.
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DR EMBL; CP021744; ARZ67446.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z2KZK2; -.
DR KEGG; salj:SMD11_1785; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000195755; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd16928; HATPase_GyrB-like; 1.
DR CDD; cd00822; TopoII_Trans_DNA_gyrase; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR002288; DNA_gyrase_B_C.
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 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; 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};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ARZ67446.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 479..593
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 706 AA; 77232 MW; CB4348512D49DECB CRC64;
MTAEMSVPST ALLTGADRDG SNYTARHLLV LEGLEAVRKR PGMYIGSTDS RGLMHCLWEI
IDNSVDEALG GFCDRIDVIL HDDGSVEVRD NGRGIPVDVE PKTGLSGVEV VMTKLHAGGK
FGGGSYAASG GLHGVGASVV NALSARLDVE VDRNSRTHAI SFRRGVPGIF TESGPDAPFD
PGNGLLKGKK VPKTRTGTRV RYWADRQIFL KDAKLSLETL YGRARQTAFL VPGLTIVVRD
ERGLDGEGAT EETFRYDGGI SEFCEYLAQD KAVCDVLRLT GQGTFKETVP VLDDRGHMTP
TEVTRELGVD IALRWGTGYD SSVKSFVNII ATPKGGTHVS GFERSITKTV NEVLRSSKLL
RVAEDDVVKD DAMEGLTAVV TVRLAEPQFE GQTKEVLGTS AATRIVANVV AKELKAFLTS
TKRDAKQQAR AVMEKVVAAA RTRIAARQHK EAQRRKTALE SSSLPAKLAD CRSDDVERSE
LFIVEGDSAL GTAKLARNSE FQALLPIRGK ILNVQKSSVS DMLKNAECGA IIQVIGAGSG
RTFDIDAARY GKVIFLADAD VDGAHIRCLL LTLFQRYMRP MVEEGRVFSA VPPLHRVELT
RPKKGQDKYI YTYSDSELRQ TLLELERKNI PYKDGIQRYK GLGEMDADQL AETTMDPRHR
TLRRINISDL EAAERAFDLL MGNEVAPRKE FITNSAATLD RSRIDA
//
