ID A0A1H8C3A9_9BACT Unreviewed; 650 AA.
AC A0A1H8C3A9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=SAMN04487902_104267 {ECO:0000313|EMBL:SEM88934.1};
OS Prevotella sp. ne3005.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1761887 {ECO:0000313|EMBL:SEM88934.1, ECO:0000313|Proteomes:UP000199132};
RN [1] {ECO:0000313|Proteomes:UP000199132}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NE3005 {ECO:0000313|Proteomes:UP000199132};
RA Varghese N., Submissions S.;
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; FOCK01000004; SEM88934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8C3A9; -.
DR STRING; 1761887.SAMN04487902_104267; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000199132; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd01030; TOPRIM_TopoIIA_like; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR002288; DNA_gyrase_B_C.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR001241; Topo_IIA.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR000565; Topo_IIA_B.
DR InterPro; IPR013759; Topo_IIA_B_C.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR006171; TOPRIM_domain.
DR PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR PANTHER; PTHR45866:SF2; DNA TOPOISOMERASE (ATP-HYDROLYZING); 1.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF00986; DNA_gyraseB_C; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
DR PRINTS; PR01159; DNAGYRASEB.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00433; TOP2c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:SEM88934.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000199132}.
FT DOMAIN 415..525
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT COILED 352..379
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 650 AA; 74337 MW; F2F2E8AFCC112E1F CRC64;
MIEDNSIISQ PNEQVNYDED NIRHLSDVDH IRTRPGMYIG RLSDGSQPED GIYVLLKETI
DNSVDEFRMN AGKRIEIDII DHLRVSVRDY GRGIPQGKII EAVSQLNTGG KYDSKAFKKS
VGMNGVGIKA VNFLSSHFEA HSYRDGQVRK VVFERGILKS DVTEPSNDET GTYIMFEPDD
TLFKNYSYRD EIIENMLRNY TYLNSGLAIM YNGRRIISRN GLEDLLTDRM TNDGLYPIVH
LKGEDIEIAF THSDQYGEEY YSFVNGQHTV QGGTHQSALK EHIAKTIKEY FGKYEPGDIR
TGIVAAIALN VEEPTFESQT KIKLGSTQMS PNGVSINKYV GDFIKQEVDN YLHIHQDVAE
ALETKIKESE RERKEMAGIT KKARERAKKA NLHNRKLRDC RIHYNDAKND RKEESSIFIT
EGDSASGSIT KSRDVNTQAV FSLRGKPLNT FKLTKKVVYE NEEFNLLQAA LDIEDGLDNL
RYNKVIVATD ADVDGMHIRL LLITFFLKFF PELIKKGHVY VLQTPLFRVR NRRTKIKNKK
VIAEADAKSG KKGDFITRYC YSDEERLTAV SELGPDPEIT RFKGLGEISP DEFAGFIGPD
IRMEQVTLHK NDQIQKLLEY YMGDNTMERQ NFIIDNLVVE EDRPEEESYD
//
