ID J6H0P0_9PORP Unreviewed; 648 AA.
AC J6H0P0;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=HMPREF1323_1472 {ECO:0000313|EMBL:EJU16723.1};
OS Porphyromonas sp. oral taxon 279 str. F0450.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1125723 {ECO:0000313|EMBL:EJU16723.1, ECO:0000313|Proteomes:UP000004156};
RN [1] {ECO:0000313|EMBL:EJU16723.1, ECO:0000313|Proteomes:UP000004156}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0450 {ECO:0000313|EMBL:EJU16723.1,
RC ECO:0000313|Proteomes:UP000004156};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) 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:EJU16723.1}.
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DR EMBL; ALKJ01000019; EJU16723.1; -; Genomic_DNA.
DR RefSeq; WP_009432877.1; NZ_ALKJ01000019.1.
DR AlphaFoldDB; J6H0P0; -.
DR PATRIC; fig|1125723.3.peg.952; -.
DR Proteomes; UP000004156; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000004156}.
FT DOMAIN 410..520
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 648 AA; 73692 MW; D75A5D8080687D6A CRC64;
MTLLEQTTVD YNDSDIKTLE WDEHIRRRPG MYIGKLGDGS HSDDGIYVLL KEVLDNSIDE
YVMGAGKKVE ITIREGQVTV RDYGRGIPLG KLIDATSKMN TGGKIDSKAF KKSVGLNGVG
IKAVNALSIH CEITVWREGL TKTVRYSHAK LLEETEAVPS DEPSGTRVVF RPDADLFRDY
EYKDEFVETM VKNYSFLNAG LALIYNGKRY LSKRGLADLL EENITEEPLY PIIHLKEDDV
EIVLTHTSQV GEDFYSFVNG QNTTQGGTHL SAFKEAVARV IKDFFGKNFD YRDIRYGMAA
AISIKIEEPV FESQTKTKLG SKDMEPDGRS IQKFLNDFLG KELDNYLHIH PEDAAIMLQK
IQESERERKS LSGVAKLARE RAKKASLHNK KLRDCTIHFN DPKAKEPERT SLFITEGNSA
SGSITTCRDP KYQAVFSLRG KPLNCYGQSK KVVYENEEFN LLQAALNIED GLDGLRYNRI
IIATDADDDG MHIRLLLITF FLQFFPELVR RGHVFILETP LFRVFLPKEH KKSDNFMTST
PAKKKGRTKK TAEEAPAEEL VTNIYCYNEA QKQAALKKLG KRALVTRFKG LGEISPEQFK
DWISEENIKL DPIRIRKEDN LSNLLMFYMG KNTPERQNFI IDNLVVDE
//