ID J6IGW6_9FLAO Unreviewed; 617 AA.
AC J6IGW6;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=HMPREF1154_1807 {ECO:0000313|EMBL:EJU31538.1};
OS Capnocytophaga sp. CM59.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=936370 {ECO:0000313|EMBL:EJU31538.1, ECO:0000313|Proteomes:UP000003140};
RN [1] {ECO:0000313|EMBL:EJU31538.1, ECO:0000313|Proteomes:UP000003140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM59 {ECO:0000313|EMBL:EJU31538.1,
RC ECO:0000313|Proteomes:UP000003140};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) 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 -!- 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:EJU31538.1}.
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DR EMBL; ALNN01000015; EJU31538.1; -; Genomic_DNA.
DR RefSeq; WP_009641389.1; NZ_ALNN01000015.1.
DR AlphaFoldDB; J6IGW6; -.
DR PATRIC; fig|936370.3.peg.1037; -.
DR Proteomes; UP000003140; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd00822; TopoII_Trans_DNA_gyrase; 1.
DR CDD; cd01030; TOPRIM_TopoIIA_like; 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; 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; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR PANTHER; PTHR45866:SF2; DNA TOPOISOMERASE (ATP-HYDROLYZING); 1.
DR Pfam; PF00204; DNA_gyraseB; 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 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 414..524
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT COILED 358..385
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 617 AA; 70404 MW; 00DF242ADA633832 CRC64;
MEPIDFNKSI TEYGEDNIQT LEWQEHVRMR PGMYIGKLGD GSSADDGIYI LLKEVIDNSI
DEFVMGAGKQ IEVRIEDNKV TVRDFGRGIP LGKVVDVVSK MNTGGKYDSR AFKKSVGLNG
VGTKAVNALS SYFYVASVRD GQRKSATFSL GVLQEESPLE ASNEKRGTLV TFVPDGTIFK
NYKFRSEYVV RMLKNYTYLN PGLTIVYNGE KFFSENGLED LLKEDNNEED FAYPIIHLSG
EDIEIALTHS KSQYSEQYYS FVNGQNTTQG GTHLNAYREA IVATLRNYYN KPYEASDIRK
SIIGAISIKV MEPVFESQTK TKLGSTEMGE GMPSVRTYIT NFVQKHLDDY LHKQPEIAEE
IQKKILQAER ERKELSDIRK LARDRAKKVS LHNKKLRDCR IHLTDSKHEQ ALESTLFITE
GNSASGSITT SRDANTQAVF SLRGKPLNSF GKTKKIVYEN EEFNLLQAAL DIEDSIENLR
YNNIVLATDA DVDGMHIRLL LITFFLQFFP ELIKEGHVYI LQTPLFRVRN SKETIYCYTD
EERVNAIAKL KNPEITRFKG LGEISPDEFK HFIGQDMRLD PVMMDKAMHI EKLLDFYMGN
NTPERQDFII NNLKYEV
//
