ID A0A1I5GYB0_9BACT Unreviewed; 631 AA.
AC A0A1I5GYB0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=SAMN04488519_106126 {ECO:0000313|EMBL:SFO40571.1};
OS Algoriphagus ornithinivorans.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=226506 {ECO:0000313|EMBL:SFO40571.1, ECO:0000313|Proteomes:UP000199564};
RN [1] {ECO:0000313|Proteomes:UP000199564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15282 {ECO:0000313|Proteomes:UP000199564};
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOVW01000006; SFO40571.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5GYB0; -.
DR STRING; 226506.SAMN04488519_106126; -.
DR Proteomes; UP000199564; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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 CDD; cd00822; TopoII_Trans_DNA_gyrase; 1.
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; 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; 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; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
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 Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:SFO40571.1}.
FT DOMAIN 409..519
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 631 AA; 71987 MW; EE0C577D9D3BCE58 CRC64;
MAETVKYTED SIKSLDWREH IRLRPGMYIG KLGDGSAQDD GIYVLVKEVL DNSIDEHMMG
YGRTIEVKIS EHRVEIRDYG RGIPLGKVID CVSKINTGGK YDSGAFQKSV GLNGVGTKAV
NALSDYFKVQ SYRDGETKIA EFEKGVLKED KPIEKSSDRN GTKVIFTPDA GIFKNYHFIP
EYLENQIWNY AYLNAGLTIN FNGKKFFSDR GLYDLLSNKV DEESSRYPII HLKGNDIEVA
ITHSNQYGEE YYSFVNGQYT TQGGTHLAAF REAIVKTVRE FYKKDYDSSD IRQSVVAAIA
VRVQEPVFES QTKTKLGSQS VGPEGPTLRT FVNDFIKTEL DNYLHKNPAV ADALLKRILQ
SERERKEISG IKKLANERAK KANLHNKKLR DCRVHYDDAK ANEDLKNNTM LFITEGDSAS
GSITKSRDVQ TQAVFSLRGK PLNCFGMTKK VVYENEEFNL LQHALNIEDG IENLRYRKIV
IATDADVDGM HIRLLIMTYF LQFFPDLVKN GHLFILDTPL FRVRNKKETI YCYSDEERQR
AIHKLGNKPE ITRFKGLGEI SPEEFGTFIG EDIRLEPIIL NKETKISDLL NFYMGKNTPD
RQNFIIDNLK IEKDLALDDP RKNDEPEEEA A
//