ID A0A259K7T2_9GAMM Unreviewed; 704 AA.
AC A0A259K7T2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
DE Flags: Fragment;
GN ORFNames=B7X52_06460 {ECO:0000313|EMBL:OZA95835.1};
OS Thiotrichales bacterium 34-46-19.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales.
OX NCBI_TaxID=1970605 {ECO:0000313|EMBL:OZA95835.1, ECO:0000313|Proteomes:UP000216156};
RN [1] {ECO:0000313|EMBL:OZA95835.1, ECO:0000313|Proteomes:UP000216156}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=34-46-19 {ECO:0000313|EMBL:OZA95835.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) 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 -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000256|ARBA:ARBA00008263}.
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:OZA95835.1}.
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DR EMBL; NCJU01000128; OZA95835.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A259K7T2; -.
DR Proteomes; UP000216156; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd00187; TOP4c; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 2.120.10.90; DNA gyrase/topoisomerase IV, subunit A, C-terminal; 1.
DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
DR InterPro; IPR006691; GyrA/parC_rep.
DR InterPro; IPR035516; Gyrase/topoIV_suA_C.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR013758; Topo_IIA_A/C_ab.
DR InterPro; IPR013757; Topo_IIA_A_a_sf.
DR InterPro; IPR002205; Topo_IIA_dom_A.
DR NCBIfam; TIGR01063; gyrA; 1.
DR PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR Pfam; PF03989; DNA_gyraseA_C; 3.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 11..497
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT NON_TER 704
FT /evidence="ECO:0000313|EMBL:OZA95835.1"
SQ SEQUENCE 704 AA; 78406 MW; 50E262460CB1FA68 CRC64;
MSEIAKEIIS VSLEGEMKQS YLDYAMSVIV GRALPDVRDG LKPVHRRVLY AMSELGNDWN
KAYKKSARVV GDVIGKYHPH GDTAVYDTIV RMAQDFSMRY VLVDGQGNFG SVDGDSPAAM
RYTEVRMARL AHELLADLEK DTVDFSPNYD GSEHEPVVFP SRIPNLLING QTGIAVGMAT
NIPPHNLTEV VNATIALLDR PSLTVAELMQ HVPAPDFPTA GIIYGVGGLR DAYETGRGRV
VMRARAHFEE KNNKNQIVVT ELPYQVNKAK LIERIAEMVK EKQIDGITGL RDESDKDGMR
MVVEVRRGES LEVLLNQLYK TTAMQTAFNF NMVAIVDGQP RLLNLKQILE FFIRHRREVV
TRRSRFELRK ARDRAHLLEG LTVALSNVDE MIAIIKASPT PPLAKQALLE RGWSADKVME
LLSRAEEVST RPEHISAEFG MRADGYYLSP EQAQAILDLR LQRLTGLEQD KIFAEYGELL
NTMLALLEIL RNPVRLTEVV REELVAVVTQ YGDKRRSEIE FNALDMSRED LIPQEDLIVT
LSDDGYIKAQ PTSDYRAQRR GGRGKAAASV KESDSVGRVI VAHSHATLLC FSNRGKLYWL
RTFDIPQAGR TARGRPINNL LPLEGDELIT SILPVSAFEA GQYVFMATSA GVVKKTELMD
FSRPRASGII ALGLDDGDAL VQAVLTTGDN DVMLLADNGK AIRF
//
