GenomeNet

Database: UniProt
Entry: A0A401I276_9BACL
LinkDB: A0A401I276_9BACL
Original site: A0A401I276_9BACL 
ID   A0A401I276_9BACL        Unreviewed;       661 AA.
AC   A0A401I276;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   08-NOV-2023, 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=PA598K_03787 {ECO:0000313|EMBL:GBF75384.1};
OS   Paenibacillus sp. 598K.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1117987 {ECO:0000313|EMBL:GBF75384.1, ECO:0000313|Proteomes:UP000288287};
RN   [1] {ECO:0000313|EMBL:GBF75384.1, ECO:0000313|Proteomes:UP000288287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=598K {ECO:0000313|EMBL:GBF75384.1,
RC   ECO:0000313|Proteomes:UP000288287};
RA   Mizushima D., Miyazaki T., Shiwa Y., Kimura K., Fujita N., Yoshikawa H.,
RA   Kimura A., Kitamura S., Hara H., Funane K.;
RT   "A novel intracellular dextranase derived from Paenibacillus sp. 598K with
RT   an ability of degrading cycloisomaltooligosaccharides.";
RL   Submitted (MAR-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:GBF75384.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BFBX01000064; GBF75384.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401I276; -.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000288287; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
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; 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; IPR005740; ParE_type2.
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   NCBIfam; TIGR01058; parE_Gpos; 1.
DR   PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR   PANTHER; PTHR45866:SF12; DNA TOPOISOMERASE 4 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   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:GBF75384.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288287}.
FT   DOMAIN          439..553
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          403..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..420
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   661 AA;  73427 MW;  66820A58FB9FE431 CRC64;
     MTEQVNNVNA ATVQERGYDA EDIQILEGLT AVRKRPGMYI GSTTTSGLHH LVWEIVDNAV
     DEHLAKFCSE IDVIIHTDQS VTVKDNGRGI PTGMHKTGIP TPQVVFTILH AGGKFGGGGY
     KKSGGLHGVG ASVTNALSEW LEVEIARDGK LHKQRFAYWV DEAGVEHVGE PVTTLEVVGK
     ANRTGTKVTF KPDTRVFHGN IAINFDTLSE RLQEIAFLNS GLKVTVKDER ADKHEVFHYE
     GGARQFVQFL NEDKAVLHDV IHFAAERDEI EVEVAMQYND GYTETIASFV NSIPTRGGGT
     HETGFKTAYT RAMNEYARKT SLLKEKDKNL DGADLREGMM AVINIKMAEV EFVGQTKDQL
     GSASARSAVD AIVSDKMQVF LEENPQVGQQ LIKKAVQASR AREAARKARD EIRSGKKRSE
     SSNLGGKLTP AQSKDYTRNE LFIVEGDSAG GSAKQGRDSK HQAILPLKGK PMNPEKAKLV
     DILKNDEYKA IIAAIGAGVG SEFDASEGNY NKIIIMTDAD TDGAHIQVLL LTFFYRYMKP
     LIDAGRVYIA QPPLYKISSK SGKHTTIRYA FTDEQLQNYL KEFKSYELQR YKGLGEMNPD
     QLWETTMDPE SRTLLQVQIE DAAKAERRVS TLMGDKVEPR KRWIVENVDF MEYEDPEGIN
     Q
//
DBGET integrated database retrieval system