ID A0A1G8DH85_9FLAO Unreviewed; 885 AA.
AC A0A1G8DH85;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Topoisomerase-4 subunit A {ECO:0000313|EMBL:SDH57003.1};
GN ORFNames=SAMN04489796_103212 {ECO:0000313|EMBL:SDH57003.1};
OS Winogradskyella thalassocola.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=262004 {ECO:0000313|EMBL:SDH57003.1, ECO:0000313|Proteomes:UP000199492};
RN [1] {ECO:0000313|EMBL:SDH57003.1, ECO:0000313|Proteomes:UP000199492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15363 {ECO:0000313|EMBL:SDH57003.1,
RC ECO:0000313|Proteomes:UP000199492};
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 -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000256|ARBA:ARBA00008263}.
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DR EMBL; FNCZ01000003; SDH57003.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8DH85; -.
DR STRING; 262004.SAMN04489796_103212; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000199492; 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 Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
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 PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:SDH57003.1};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 19..454
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 852..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 419..453
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 862..878
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 885 AA; 100909 MW; 725F8ED9011C05D5 CRC64;
MIEEHDELLN EDDGSQETIT KVTGMYKEWF LDYASYVILE RAVPAIEDGF KPVQRRIMHS
MKDLDDGRYN KVANIVGHTM QYHPHGDASI ADAMVQIGQK DLLIDTQGNW GNILTGDRAA
ASRYIEARLS KFALDVVYNP KITEWQSSYD GRRKEPINLP VMFPLLLAQG GEGIAVGLST
KILPHNFIEL IDASVKHLKG KRFTILPDFP TAGIADFTNY NDGLRGGKVR VRALISQRDK
NTLMITEIPF GTTTTSLIDS ILKANEKGKI KIKKIEDNTA AEVEILIHLP SGLSPDKTID
ALYAFTSCES SISPLGCVIE DNKPYFVGVT EMLRRSTDNT VQLLKSELEI RLAEFQEQWH
FASLERIFIE KRIYRDIEEE ETWDGVIDAI DKGLQPHIKH LKRAITVEDI TRLTEIRIKR
ISKFDIDKAQ QKIDALEDQI AEVKHHLANL IDYAIAYFER LKKDYGEGKE RKTEIRIFDD
VDATKVVIRN TKLYVNREEG FVGTALKRDE YVCDCSDIDD IIVFTDQGTM MVTKVDSKTF
IGKNIIHVAV FKKKDKRTIY NLIYRDGKGG PSYVKRFAVT SMTRDREYDL TNGSKGSALW
YFSANPNGEA EVVTIMLRQV GSIKKLKWDL DFAEVLIKGR ASKGNRVTKY AIKRVELKER
GVSTLKPRKI WFDDTVQRLN VDNRGELIGE FRGEDRLLVI NQSGVVKTII PELTTHFDSD
MIVLEKWIPK KPISAIYYDG EKERYYVKRF IIEQEGREED FISDHPDSQL EIVSTDWRPM
ADVEFTKERG KERKPNMEVD LEEFISVKGV NALGNQLTKD KINQISLLES LPYEAPEEVP
ADEIEVVDEE TVDVVESQSE SGNSSKDDDD DHDLGMDEKG QVTLF
//