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Database: UniProt
Entry: A0A239XC55_9SPHI
LinkDB: A0A239XC55_9SPHI
Original site: A0A239XC55_9SPHI 
ID   A0A239XC55_9SPHI        Unreviewed;       631 AA.
AC   A0A239XC55;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=SAMN05192578_103110 {ECO:0000313|EMBL:SDL38234.1};
OS   Sphingobacterium mizutaii.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=1010 {ECO:0000313|EMBL:SDL38234.1, ECO:0000313|Proteomes:UP000199201};
RN   [1] {ECO:0000313|EMBL:SDL38234.1, ECO:0000313|Proteomes:UP000199201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11724 {ECO:0000313|EMBL:SDL38234.1,
RC   ECO:0000313|Proteomes:UP000199201};
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; FNGK01000003; SDL38234.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239XC55; -.
DR   STRING; 1010.SAMN05192578_103110; -.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000199201; 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:SDL38234.1}.
FT   DOMAIN          402..512
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   631 AA;  71373 MW;  07436CF44D1CC7D5 CRC64;
     MSTYNEDSIR SLDWKEHIRL RPGMYIGKLG DGSAYDDGIY VLLKEVVDNS IDEFVMGAGK
     IIDITVNENR VTVRDYGRGI PIGSVVDVVS KINTGGKYDS KAFQKSVGLN GVGTKAVNAL
     SNQFSVQSYR QNVTRIAQFS KGELVSDEQK DTTQRNGTSV TFYPDDSIFR NYKYRLEFVE
     NMIWNYVFLN SGLTINFNGQ RFISENGLKD LLERNVDTEG MRYPIIHLKG DDIEIAMTHG
     QQYGEEYYSF VNGQHTTQGG THQAAYREAV VKTIREFYKK EFDASDVRAS IIGAIAIKVQ
     EPVFESQTKT KLGSQSVGPD GPTVRTFIND FVKKALDDYL HKNPATADAL QKRIMQSERE
     RKDIAGIKKL ANERAKKASL HNRKLRDCKV HFSDKHERNL ETTLFITEGD SASGSITKSR
     DVYTQAVFSL KGKPLNSYGL TKKIVYENEE FNLLQHALNI EDGIEGLRYN NIVIATDADV
     DGMHIRLLLM TFFLQFFPEL VKAGHVSILQ TPLFRVRNKK ETIYCYSDEE RVNAIKKLGA
     KPEITRFKGL GEISPSEFGM FIGENIRLEP VILSKDNKLP QLLEYYMGKN TPDRQVHIVN
     NLRVELDTED DLVTTKDGVE EAAIESIQEA V
//
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