ID A0A1M3EI95_9CELL Unreviewed; 709 AA.
AC A0A1M3EI95;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=BGO38_08380 {ECO:0000313|EMBL:OJV58199.1};
OS Cellulomonas sp. 73-145.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1895739 {ECO:0000313|EMBL:OJV58199.1, ECO:0000313|Proteomes:UP000184491};
RN [1] {ECO:0000313|EMBL:OJV58199.1, ECO:0000313|Proteomes:UP000184491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=73-145 {ECO:0000313|EMBL:OJV58199.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJV58199.1}.
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DR EMBL; MKTI01000009; OJV58199.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3EI95; -.
DR STRING; 1895739.BGO38_08380; -.
DR Proteomes; UP000184491; Unassembled WGS sequence.
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:OJV58199.1};
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 481..595
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 709 AA; 77013 MW; BA1F28D75A67C6F4 CRC64;
MTTVSSQSGY TARHLSVLEG LEAVRKRPGM YIGTTDSRGL MHCLWEIIDN AVDEALGGFC
RHIEVVLHAD SSVEVRDDGR GIPVDVEPKT GLTGVEVVFT KLHAGGKFGG GSYAASGGLH
GVGASVVNAL SARLDVEVDR HGRTHLMTFH RGEPGLFDDS AGRGPESPFQ PFVSGSDLAV
TGKVGKAVTG TRVRYWADPQ IFPSTAAFSY DELATRARQT SFLVPGLEIV LRDERGLAGT
PGEHGPHTET FVHTGGVVDF VEHLAPDQPV TDIWRLVGSG DFVETVPVLD ERGHMVPREV
TRTCDVEVAV RWGTGYETDV RSFVNIIATP KGGTHVAGFE QALLKTLREQ VAANARRLKV
STKDTTERLE KDDIMAGLTA VVTVRLAEPQ FEGQTKEVLG TGPVRGIVAK VVATELGTML
TSTRNPAKTQ AATLLDKLVG EMHARLSARK QKEISRRKTA LESSSLPPKL ADCRIDDVAR
SELFIVEGDS ALGTAKLARS SDYQALLPIR GKILNVQKAS VSDMLKNAEC AAILQVVGAG
SGRTFDLEAA RYGKIILMTD ADVDGAHIRT LLLTLFFRYM RPLVADGRVY AAVPPLHRIE
LLGGRRDDPE RYVYTYSEAE LATTLKKLDR AGKRYSPDIQ RYKGLGEMDA QQLAETTMDP
RRRTLRRVTV AAAERAEQVF ELLMGSEVGP RKDFIVAGAD ALDRNRIDA
//
