ID A0A1Q7EDN5_9CHLR Unreviewed; 699 AA.
AC A0A1Q7EDN5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=AUH44_01395 {ECO:0000313|EMBL:OLC11809.1};
OS Chloroflexi bacterium 13_1_40CM_68_15.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1805083 {ECO:0000313|EMBL:OLC11809.1, ECO:0000313|Proteomes:UP000187402};
RN [1] {ECO:0000313|EMBL:OLC11809.1, ECO:0000313|Proteomes:UP000187402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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 -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC {ECO:0000256|ARBA:ARBA00010708}.
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:OLC11809.1}.
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DR EMBL; MNEP01000026; OLC11809.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7EDN5; -.
DR Proteomes; UP000187402; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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; IPR006171; TOPRIM_domain.
DR PANTHER; PTHR45866:SF1; DNA GYRASE SUBUNIT B, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE 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; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:OLC11809.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 428..542
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 83..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 699 AA; 76883 MW; 98CB0D7EEDE237B8 CRC64;
MAVRKEPPKT TKRGSYGASD IQVLEGLEAV RRRPGMYIGT TDLRGLHHLV REVLDNSIDE
AMNGTCDRID VWIGESNEIT VADNGRGIPV GPHPTQKDPR GRPMDALEVV MTILHAGGKF
GGAGYKVSGG LHGVGVSVVN ALASGTVVEV HRDIPKPQLP IPPVLPWKES GRATGTVTRF
APDKEMFPVI EWDAGIITQW LRETAYLNKS LWLALHDERT GAEENYYFDG GVISFVRHLN
RSHQNLHPKP VYVERTFDNA TVVEVALQYN DSFAEKVYTF ANNINTIDGG AHLTGFRTAL
TRTINAYARK SGALKESDPN LTSDDVREGL TAVISVKIRE PQFEGQTKTR LGNAEIAGQV
AAAVNDALGA YLEENPPDAK RIVEKSLTAF RAREAARKAR DVFRKGALDG FSLPGKLADC
SERDPEKCEL FIVEGPSAGG SAKAGRDRRT QAILPLKGKI LNVEKARADK MLGNEEIKAL
ITALGTGIGD YFDVKKLRYG QTILLCDADV DGSHIRTLLL TLLYRHFRPL IEDGRIYIGQ
PPLYRLQLGK EVRWAYSDHE RDKAIKELKS VAKTKRDDRK KAAGDKAEAD GDKATSRARR
RAAEEAEDQV ETTSTNTDEG TDDGKGGREP AIARYKGLGE MNAEQLWDTT LNPATRTLKR
VTLEDAELAD LVFDELMGSE VEGRKKWIMA NADKAALDI
//
