ID   A3XNX9_LEEBM            Unreviewed;       875 AA.
AC   A3XNX9;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=DNA topoisomerase IV subunit A {ECO:0000313|EMBL:EAQ48746.1};
GN   ORFNames=MED217_09365 {ECO:0000313|EMBL:EAQ48746.1};
OS   Leeuwenhoekiella blandensis (strain CECT 7118 / CCUG 51940 / KCTC 22103 /
OS   MED217) (Flavobacterium sp. (strain MED217)).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Leeuwenhoekiella.
OX   NCBI_TaxID=398720 {ECO:0000313|EMBL:EAQ48746.1, ECO:0000313|Proteomes:UP000001601};
RN   [1] {ECO:0000313|EMBL:EAQ48746.1, ECO:0000313|Proteomes:UP000001601}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED217 {ECO:0000313|EMBL:EAQ48746.1,
RC   ECO:0000313|Proteomes:UP000001601};
RX   PubMed=17215843; DOI=10.1038/nature05381;
RA   Gomez-Consarnau L., Gonzalez J.M., Coll-Llado M., Gourdon P., Pascher T.,
RA   Neutze R., Pedros-Alio C., Pinhassi J.;
RT   "Light stimulates growth of proteorhodopsin-containing marine
RT   Flavobacteria.";
RL   Nature 445:210-213(2007).
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:EAQ48746.1}.
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DR   EMBL; AANC01000007; EAQ48746.1; -; Genomic_DNA.
DR   RefSeq; WP_009780249.1; NZ_CH672395.1.
DR   AlphaFoldDB; A3XNX9; -.
DR   STRING; 398720.MED217_09365; -.
DR   eggNOG; COG0188; Bacteria.
DR   HOGENOM; CLU_015760_0_0_10; -.
DR   OrthoDB; 9806486at2; -.
DR   Proteomes; UP000001601; 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:EAQ48746.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001601};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          23..457
FT                   /note="DNA topoisomerase type IIA"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   REGION          832..875
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          341..368
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          422..456
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        835..863
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   875 AA;  99827 MW;  993AD3031C1DF8BB CRC64;
     MSENYEDPNL DQPEDENSGE TITRVTGMFK DWFLDYASYV ILERAVPAIE DGFKPVQRRI
     MHSMKDLDDG RYNKVANIVG HTMQYHPHGD ASIADAMVQM GQKDLLIDTQ GNWGNTLTGD
     SAAASRYIEA RLSKFALEVL FSPKITDWQA SYDGRRKEPI NLPVKFPLLL AQGAEGIAVG
     LSTKVLPHNF VELIDASVKH LEGKKFKILP DFPSAGEADF SDYKDGKRGG RIRVRAKISQ
     LDKNTLVITE IPFTTTTTSL IDNILKANDK GKLKIKRIED NTSSQVEILV HLPAGLSPDK
     TIGALYAFTN CEVSISPLGC VIEDNKPLFV GVSEMLRIST DRTKDLLRQE LEIQLEELEN
     QWHYASLERI FIENRIYRDI EEETTWDGVL HAINEGLKPH IGHLKRPVVE EDLVRLTEIR
     IKRISKFDID KAQQRIEALE DQIAEVKHHL EHLTDYAIAY FKRLKKEFGA GRERKTEIKL
     FDDIEASKVV IRNTKLYVNR KEGFVGTSLK KDEYVTDCAD IDDIIVFTKE GVMMVTKVDT
     KTFVGKDIIH VAVFKKKDKR TIYNMLYRDG KGGATYVKRF NVTSVTRDRE YDMTKGKKGS
     QVLYFSANPN GEAEVVSVYL RAVGNIKKLK FDLDFSDILI KGRNANGNLA TKHSVRTIEL
     KEKGVSTLKP RKIWFDDTVQ RLNVDGRGEL LGEFKGEDRL LIITQDGVVK TITPELTTRF
     DTKMIVLEKW IPNKPISAIY WDGNRERYYV KRFLIENPEK EEVFVSDHAD TQLEIVSTDY
     RPVVEMVFYK ERNKDQKPNE SVDIEEFIAI KGINALGNQF YTEKLKQINL LDPLPYEEEP
     EEEPEQEVIE SDSESEVTPE EDDDVKGDGT QGSLF
//