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Database: UniProt
Entry: A0A1D7XPG1_9FLAO
LinkDB: A0A1D7XPG1_9FLAO
Original site: A0A1D7XPG1_9FLAO 
ID   A0A1D7XPG1_9FLAO        Unreviewed;       898 AA.
AC   A0A1D7XPG1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=DNA topoisomerase IV subunit A {ECO:0000313|EMBL:AOR25218.1};
GN   ORFNames=FORMA_00200 {ECO:0000313|EMBL:AOR25218.1};
OS   Formosa sp. Hel3_A1_48.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Formosa.
OX   NCBI_TaxID=1336795 {ECO:0000313|EMBL:AOR25218.1, ECO:0000313|Proteomes:UP000094318};
RN   [1] {ECO:0000313|EMBL:AOR25218.1, ECO:0000313|Proteomes:UP000094318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hel3_A1_48 {ECO:0000313|EMBL:AOR25218.1,
RC   ECO:0000313|Proteomes:UP000094318};
RA   Unfried F., Harder J., Teeling H., Hahnke R.L., Markert S., Kappelmann L.,
RA   Chafee M.;
RT   "Glycan utilization in Formosa spp.";
RL   Submitted (SEP-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; CP017259; AOR25218.1; -; Genomic_DNA.
DR   RefSeq; WP_069673749.1; NZ_CP017259.1.
DR   AlphaFoldDB; A0A1D7XPG1; -.
DR   STRING; 1336795.FORMA_00200; -.
DR   KEGG; foh:FORMA_00200; -.
DR   PATRIC; fig|1336795.4.peg.20; -.
DR   OrthoDB; 9806486at2; -.
DR   Proteomes; UP000094318; Chromosome.
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:AOR25218.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094318};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          21..455
FT                   /note="DNA topoisomerase type IIA"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   REGION          859..898
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          420..447
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        869..886
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   898 AA;  101496 MW;  B20349ACE4C91429 CRC64;
     MIEDQGHIPE EDHTQGQETI TRVTGMYKDW FLDYASYVIL ERAVPAIEDG FKPVQRRILH
     SMKDLDDGRY NKVANIVGHT MQYHPHGDAS IADAMVQIGQ KDLLIDTQGN WGNILTGDRA
     AASRYIEARL SKFALDVVFN PKTTEWQASY DGRRKEPINL PVKFPLLLAQ GAEGIAVGLS
     TKVLPHNFIE LIEASIKHLQ GKRFTIVPDF ATGGIADFSN YNDGLRGGKV RCRARIGQLN
     KNTLVITEVP FGTTTSSLID SILKANDKGK IKIKKIEDNT AAEVEILIHL PSGISPDKTI
     DALFAFTNCE TSISPLGCVI EDNKPLFVGV SEMLRHSTNL TVELLKLELE IRLNELEEQW
     HFASLERIFI ENRIYRDIED EETWEGVISA IDKGLQPYIQ HLKRAITTDD ITRLTEIRIK
     RISKFDIDKA QQKIEALEDQ IEETKGYLAT IIDYAIAYFK RLKADYGKGK ERKTEIKVFA
     DVDATKVVIR NTKLYVNREE GFVGTGMRRE EYVCDCSDID DIIVFTKAGK MMVTKVDTKT
     FVGKNIIHVS VFKKKDTRTI YNMIYKDGKG GASYIKRFAV TSITRDREYD LTKGKPQTNV
     LYFSANPNGE AEIVSVLLRQ VGSIKKLKWD VDFSDISIKG RASKGNIVTK HAVKRIELKE
     KGMSTLKPRK IWFDDTIQRL NVDGRGDLIG EFRGEDRLLV ITQSGLIKTI VPEITTHFSD
     DMIVLEKWIP SKPISAIYYD GAKEKYFVKR FLIENESKEE VFISAHASSA LEIVSTDWRP
     MAELTFAKDR GKDRKPNQKI NIAQFIDVKG ISAQGNQLSR QKVNQIDLLE PLPFQAPEAI
     PADELEVVDE VEISVEAHLQ QQKTLEETLP PTQDEEVQRS DDLSSGSTDP EEGQITLF
//
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