ID A0A2S1R0F7_9FLAO Unreviewed; 881 AA.
AC A0A2S1R0F7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=DNA gyrase/topoisomerase IV subunit A {ECO:0000313|EMBL:AWH86039.1};
GN ORFNames=HYN59_13370 {ECO:0000313|EMBL:AWH86039.1};
OS Flavobacterium album.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2175091 {ECO:0000313|EMBL:AWH86039.1, ECO:0000313|Proteomes:UP000244929};
RN [1] {ECO:0000313|EMBL:AWH86039.1, ECO:0000313|Proteomes:UP000244929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HYN0059 {ECO:0000313|EMBL:AWH86039.1,
RC ECO:0000313|Proteomes:UP000244929};
RA Yi H., Baek C.;
RT "Genome sequencing of Flavobacterium sp. HYN0059.";
RL Submitted (APR-2018) 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; CP029186; AWH86039.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S1R0F7; -.
DR KEGG; falb:HYN59_13370; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000244929; 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:AWH86039.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244929};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 30..464
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 429..456
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 8..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 881 AA; 100121 MW; CF7B573D10D6B889 CRC64;
MNEEEENINS FEGEHFYEKD DNPDSQDTIT KVTGMYKDWF LDYASYVILE RAVPAIEDGF
KPVQRRIMHS LRELDDGRYN KVANVVGHTM QYHPHGDASI GDAMVQIGQK ELLIDTQGNW
GNILTGDGAA ASRYIEARLS KFALEVLYSP KITPWQLSYD GRRNEPINLP VKFPLLLAQG
AEGIAVGLST KVLPHNFNEL IDASIKILKG KPFTLYPDFP TAGIADVSGY NDGMRGGRVR
VRAKIGQQDK STLVITQIPF STNTTTLIDS ILKANEKGKI KIKKIEDNTA AEVEILIHLP
PGVSPDKTID ALFAFTACET SVAPLGCVIE DHKPRFVGVS EMLRISTHRT VDLLKRELEI
ELDELEESWH FQSLERIFIE NRIYRLIEEE ETWEGVIKAI DEGLKPFTKH LKRAVTEEDI
VRLTEIRIKR ISKFDIDKAQ QKIEALEGEI EQVKHHLEHI IDFAIAYFQN LKDKYGKGRE
RKTELRSFDN IEATKVVLRN IKLYVNREEG FVGTGLKKDE YVADCSDIDD VIVFLRNGSM
IITKVDVKTF VGKDIIHVAV FDKNDKRTIY NMIYRDGKSG PSYIKRFNVS GVTRDKVYDL
TAGTKDSMVL YFSDNPNGEA ELITVLLRQV GSVKKLKFDI DFATIGIKGR ASRGNTVTKY
PIKKIELKEK GISTLKPRRI WFDDTVQRLN VDGRGELLGE FRPNDRLLII NQSGKVKTII
PELTTHFDEG MIVLEKWNPN KPISAIYYDG EKERYYVKRF LVENENKEEI FISEHDKSQL
EIVSTDYRPV AEVIFAKVKG VQKETITVDI ENFIAVKGIK ALGNQLTADK VKQINLLDPL
PYEEPEEVVP EEIEVKDGVD ITDENTTITL DEDGQITLSL E
//
