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Database: UniProt
Entry: A0A368MW92_9FLAO
LinkDB: A0A368MW92_9FLAO
Original site: A0A368MW92_9FLAO 
ID   A0A368MW92_9FLAO        Unreviewed;       632 AA.
AC   A0A368MW92;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=DQ356_10180 {ECO:0000313|EMBL:RCU42286.1};
OS   Chryseobacterium lacus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=2058346 {ECO:0000313|EMBL:RCU42286.1, ECO:0000313|Proteomes:UP000252172};
RN   [1] {ECO:0000313|EMBL:RCU42286.1, ECO:0000313|Proteomes:UP000252172}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YLOS41 {ECO:0000313|EMBL:RCU42286.1,
RC   ECO:0000313|Proteomes:UP000252172};
RA   Li C.-M.;
RT   "Chryseobacterium lacus sp. nov., isolated from lake water.";
RL   Submitted (JUL-2018) 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:RCU42286.1}.
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DR   EMBL; QPIE01000007; RCU42286.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A368MW92; -.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000252172; 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; 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   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:RCU42286.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000252172}.
FT   DOMAIN          414..524
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   632 AA;  72716 MW;  DF73C8B8FF00D623 CRC64;
     MNENTTVQYN EDNIKTLEPR EHVRLRPGMY IGKLGDGSAS DDGIYILLKE VIDNSIDEFR
     MKYGKKIEVK IKDGRVVIRD YGRGIPLGKI VEVVSIMNTG GKYDDGAFKK SIGLNGVGTK
     AVNFLSEYFQ VKSVREGKMR RAEFQDGKLI ELHDEAETTE RNGTEITFIP DETIFINYKF
     RSEYVERMLR NYSYLNLGLK IYYNGEVFES QNGLKDLLEE EIDSEIVYPI IHIKDEDMEI
     AITHSDKSQS ETYFSFVNGQ YTSQGGTHLN AFKEAYVKTI REFYGKNFEA ADIRKAIIGA
     VYINIGNPVF ESQTKTKLGS STMGQDKNGN ELETIKTFMI NYMKGKLDNY LHKNPEVAEA
     IQRKILISER ERKELSGIQK LARERAKKVS LHNKKLRDCR QHYNDQKASR KAESQIFITE
     GDSASGSITK SRDVETQAVF SLRGKPLNSY GLTKRVVYEN EEFNLLQAAL NIEDSLEDLR
     YNQVIIATDA DVDGMHIRLL MITFFLQFFP DLIKNGHLYI LQTPLFRVRN KKETRYCYSD
     AERIKALNEL GKNPEITRFK GLGEISPDEF KHFIGKDIRL EPVVLGKDQT IEQLLEFYMG
     KNTPDRQTFI LQNLVVENLD IDQKQKLEEV EV
//
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