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Database: UniProt
Entry: A0A1M7A3L4_9FLAO
LinkDB: A0A1M7A3L4_9FLAO
Original site: A0A1M7A3L4_9FLAO 
ID   A0A1M7A3L4_9FLAO        Unreviewed;       616 AA.
AC   A0A1M7A3L4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=SAMN05443634_108156 {ECO:0000313|EMBL:SHL37304.1};
OS   Chishuiella changwenlii.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chishuiella.
OX   NCBI_TaxID=1434701 {ECO:0000313|EMBL:SHL37304.1, ECO:0000313|Proteomes:UP000184120};
RN   [1] {ECO:0000313|Proteomes:UP000184120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27989 {ECO:0000313|Proteomes:UP000184120};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-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; FRBH01000008; SHL37304.1; -; Genomic_DNA.
DR   RefSeq; WP_072932754.1; NZ_FRBH01000008.1.
DR   AlphaFoldDB; A0A1M7A3L4; -.
DR   STRING; 1434701.SAMN05443634_108156; -.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000184120; 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   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; 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:SHL37304.1}.
FT   DOMAIN          410..516
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   COILED          347..381
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   616 AA;  70469 MW;  3EC0052932F3E84D CRC64;
     MSELNQQANY TEDNIKTLDW REHIRMRPGM YIGKLGDGSS QDDGIYILLK EIVDNCIDEF
     VMGAGKTIEI NLRDEEVTVR DYGRGIPLGK MVDAVSKMNT GGKYDSQAFK KSVGLNGVGT
     KAVNALSTNF RVQSVRDGKT RVAEFERGIL IEQEDEKETS LRKGTKITFV PDKSIFLNFK
     FRKEYVDKML KNYVYLNPGL KIIFNGEEFF SKDGLKDLLK DNIEEETIYD IIHLKGEDIE
     LAMTHSSKSY SETYYSFVNG QNTTQGGTHL AAFKEAIVKT VREFYNKNYD PADIRKSIIG
     AISIKVIEPV FESQTKTKLG SNEIGPGLST VRTFVNDFIK TNLDNFLHKN IEVAQAIERK
     IKQSENERKE LSGIRKLARD RAKKVSLHNK KLRDCRQHYN DAKAELRLDS TIFITEGDSA
     SGSITKSRSV ETQAVFSLRG KPLNSYGLSK KIVYENEEFN LLQAALNIEE GLEDLRYNNV
     VIATDADVDG MHIRLLIITF FLQFFPELIK EGHLYILQTP LFRVRNKKET RYCYSEEERL
     KALEEVKNPE ITRFKGLGEI SPDEFKHFIG KDIRLEPVMI GKDQTIDELL EFYMGKNTPT
     RQEFIINNLA IETIKN
//
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