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Database: UniProt
Entry: A0A150X519_9BACT
LinkDB: A0A150X519_9BACT
Original site: A0A150X519_9BACT 
ID   A0A150X519_9BACT        Unreviewed;       622 AA.
AC   A0A150X519;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, 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=AWW68_14095 {ECO:0000313|EMBL:KYG73800.1};
OS   Roseivirga spongicola.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Roseivirgaceae;
OC   Roseivirga.
OX   NCBI_TaxID=333140 {ECO:0000313|EMBL:KYG73800.1, ECO:0000313|Proteomes:UP000075606};
RN   [1] {ECO:0000313|EMBL:KYG73800.1, ECO:0000313|Proteomes:UP000075606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UST030701-084 {ECO:0000313|EMBL:KYG73800.1,
RC   ECO:0000313|Proteomes:UP000075606};
RA   Selvaratnam C., Thevarajoo S., Goh K.M., Ee R., Chan K.-G., Chong C.S.;
RT   "Genome sequencing of Roseivirga spongicola UST030701-084.";
RL   Submitted (JAN-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};
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:KYG73800.1}.
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DR   EMBL; LRPC01000028; KYG73800.1; -; Genomic_DNA.
DR   RefSeq; WP_068222681.1; NZ_LRPC01000028.1.
DR   AlphaFoldDB; A0A150X519; -.
DR   STRING; 333140.AWW68_14095; -.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000075606; 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; 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; 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   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:KYG73800.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075606}.
FT   DOMAIN          411..521
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   622 AA;  70464 MW;  F3CAE136AA1FB619 CRC64;
     MADQVANYTE DSIRSLDWKE HIRLRPGMYI GKLGDGSAQD DGIYVLVKEV IDNSIDEHMM
     GFGKTIDVKV SELKVEVRDY GRGIPLGKVV DCVSKINTGG KYDSGAFQKS VGLNGVGTKA
     VNALSTYFKV QSYRDGKTKV AEFERGEVKN DADETTSSGR NGTLIVFKPD ETIFKNYHFI
     PQYLDDLIWN YCFLNAGLTI NFNGVKYHSE KGLYDLLSRK TDVDSLRYPI IHLRGEDIEI
     ALSHTNQYGE DYYSFVNGQY TTQGGTHQAA LREALVKTVR EFYNKNFDAT DVRASIVGAI
     AVRVQEPVFE SQTKTKLGSQ NVAPDGPTMR TFVNEFVKKA LDDFLHKNPK TAEALQKRIL
     QSERERKEIA GIKKLANERA RKANLHNKKL RDCRIHLDDG NKVDDDLKNA TTLFITEGDS
     ASGSITKSRN VQTQAVFSLR GKPLNCYGQT KKVVYENEEF NLLQHALNIE DGLEGLRYDK
     IVIATDADVD GMHIRLLLLT YFLQFFPDLV RRGHVYILET PLFRVRNKKE TIYCYSDIER
     QKAIEKLGNK PEITRFKGLG EISPDEFKGF IGADMRLEPI ILRKDTSISD ILKFYMGKNT
     PDRQGFIIDN LRVEKDIAEE AV
//
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