ID A0A1G7YB88_CHIFI Unreviewed; 651 AA.
AC A0A1G7YB88;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=SAMN04488121_107277 {ECO:0000313|EMBL:SDG93627.1};
OS Chitinophaga filiformis (Myxococcus filiformis) (Flexibacter filiformis).
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=104663 {ECO:0000313|EMBL:SDG93627.1, ECO:0000313|Proteomes:UP000199045};
RN [1] {ECO:0000313|EMBL:SDG93627.1, ECO:0000313|Proteomes:UP000199045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 527 {ECO:0000313|EMBL:SDG93627.1,
RC ECO:0000313|Proteomes:UP000199045};
RA de Groot N.N.;
RL Submitted (OCT-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};
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DR EMBL; FNBN01000007; SDG93627.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7YB88; -.
DR STRING; 104663.SAMN04488121_107277; -.
DR Proteomes; UP000199045; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
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; 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; 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 Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:SDG93627.1}.
FT DOMAIN 438..548
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT COILED 374..401
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 651 AA; 74464 MW; 547BD710AE1DFE91 CRC64;
MESHGHCNKV NWNFYIIMAT TDKKDLLGSY TEDSIRSLDW REHIRLRPGM YIGKLGDGSS
MDDGIYILLK EVADNCIDEH TMGFGKQIDI KVTEHSVTVR DYGRGIPLGK VVDVVSKINT
GAKYDSKAFQ KSVGLNGVGT KAVNALSSYF KVESVREGRS KVAEFERGVL TKEHKETATK
EPNGTLVTFT PDDTVFRNYR FIPEFLENQI WNYCFLNAGL TINFNGTKYV SKNGLLDLLQ
RKTNEDELRY PIIHLKAEDI EVAITHENQY GEEYYSFVNG QHTTQGGTHL AAFREAFVKT
IRDFYKKDYD ATDIRASICA AISVRVQEPV FESQTKTKLG SLTVYENGPS MKAFVLDFLS
KHLDDFLHKN PTTAESLKKR IEQSERERKE LAGIKKLANE RAKKANLHNR KLRDCRFHLN
EEVSGKDKND LETKRLNTTI FITEGDSASG SITKSRNVET QAVFSLRGKP LNCFGLTKKI
VYENEEFNLL QHALNIEEGL EGLRYNRIVI ATDADVDGMH IRLLLLTFFL QFFPDLVKNG
HLYILETPLF RVRNKQQTFY CYSDEERQKA IKKLGGKPEI TRFKGLGEIS PQEFGAFINE
DMRVEPVILS TDTHIQKLLE YYMGKNTQTR QEFIISNLRY EKDLVDEPAG E
//