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Database: UniProt
Entry: A0A081PIK5_9SPHI
LinkDB: A0A081PIK5_9SPHI
Original site: A0A081PIK5_9SPHI 
ID   A0A081PIK5_9SPHI        Unreviewed;       636 AA.
AC   A0A081PIK5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=N180_09530 {ECO:0000313|EMBL:KEQ30528.1};
OS   Pedobacter antarcticus 4BY.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1358423 {ECO:0000313|EMBL:KEQ30528.1, ECO:0000313|Proteomes:UP000028007};
RN   [1] {ECO:0000313|EMBL:KEQ30528.1, ECO:0000313|Proteomes:UP000028007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4BY {ECO:0000313|EMBL:KEQ30528.1,
RC   ECO:0000313|Proteomes:UP000028007};
RA   Shivaji S., Ray M.K., Rao N.S., Saiserr L., Jagannadham M.V., Kumar G.S.,
RA   Reddy G., Bhargava P.M.;
RT   "Sphingobacterium antarcticus sp. nov. a Psychrotrophic Bacterium from the
RT   Soils of Schirmacher Oasis, Antarctica.";
RL   Int. J. Syst. Bacteriol. 42:102-106(1992).
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:KEQ30528.1}.
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DR   EMBL; JNFF01000035; KEQ30528.1; -; Genomic_DNA.
DR   RefSeq; WP_037439718.1; NZ_JNFF01000035.1.
DR   AlphaFoldDB; A0A081PIK5; -.
DR   eggNOG; COG0187; Bacteria.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000028007; 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:KEQ30528.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028007}.
FT   DOMAIN          405..515
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   636 AA;  72173 MW;  1DC086E22148F2F6 CRC64;
     MAEPIYNDDS IRSLDWKEHI RLRPGMYIGK LGDGSAQDDG IYVLLKEIMD NSIDEFVMGS
     GRTIDITVSD AKVNVRDYGR GIPLGKVIDC VSKINTGGKY DSNAFQKSVG LNGVGTKAVN
     ALSTNFVVQS YRDGKTKKVE FSKGEITVDH PIIDTTQRNG TAITFYPDES IFRNYHYIPD
     FVESMIWNYV FLNTGLTVNF NGQKYFSERG LYDLLHKVAD VENIRYPIIH LLGSDIEIAM
     THGQQYGEDY HSFVNGQHTT QGGTHQAAFR EAVVKTIREF YKKEYEASDI RASIIAAISV
     RVQEPVFESQ TKTKLGSQNM GPEGPSVRTF INDFVKKELD DYLHKHQDVA EALLKRILQS
     ERERKDIAGI KKLANDRAKK ASLHNKKLRD CKVHFNTTHD KRYETTLFIT EGDSASGSIT
     KSRDVDCQAV FSLKGKPLNC YELTKKVVYE NEEFNLLQHA LNIEDGLDGL HYNNIVIATD
     ADVDGMHIRL LMMTFFLQFF PDLVRAGHVY ILQTPLFRVR NKKETIYCYS DEERRKAIDK
     LGSRPEITRF KGLGEISPDE FGLFIGKDIR LDPVILKDQT IKNLLEYYMG KNTPDRQQHI
     IRNLRIEKDT IEELVSADAE AAIAAVTEDI VNAEPA
//
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