ID H1Y2M7_9SPHI Unreviewed; 631 AA.
AC H1Y2M7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=Mucpa_4115 {ECO:0000313|EMBL:EHQ28206.1};
OS Mucilaginibacter paludis DSM 18603.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=714943 {ECO:0000313|EMBL:EHQ28206.1, ECO:0000313|Proteomes:UP000002774};
RN [1] {ECO:0000313|EMBL:EHQ28206.1, ECO:0000313|Proteomes:UP000002774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18603 {ECO:0000313|EMBL:EHQ28206.1,
RC ECO:0000313|Proteomes:UP000002774};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Held B.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The permanent draft genome of Mucilaginibacter paludis DSM 18603.";
RL Submitted (SEP-2011) 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; CM001403; EHQ28206.1; -; Genomic_DNA.
DR RefSeq; WP_008508958.1; NZ_CM001403.1.
DR AlphaFoldDB; H1Y2M7; -.
DR STRING; 714943.Mucpa_4115; -.
DR eggNOG; COG0187; Bacteria.
DR HOGENOM; CLU_006146_1_1_10; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000002774; Chromosome.
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; 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:EHQ28206.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002774}.
FT DOMAIN 409..519
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 631 AA; 71467 MW; BFA872E41E03A0A8 CRC64;
MAENVNYDND SIRSLDWKEH IRLRPGMYIG KLGDGSAYDD GIYVLLKEIV DNSIDEFVMG
AGRSIEINMS DQKVSVRDYG RGIPLGKVID CVSKINTGGK YDSKAFQKSV GLNGVGTKAV
NALSNSFTVQ SYRDGRTKIA EFAKGELVRE EPEKETTQRN GTAINFLPDD TIFRHYRFIP
EFVDNMIWNY VYLNSGLTIN FNGQKFFSER GLYDLLVKNT DSNALRYPII HLKGEDIELA
LTHGQAYGEE YYSFVNGQHT TQGGTHQAAF REAIGKTIKE FFEKDKKDFE PVDIRASIVG
AIAIKVQEPV FESQTKTKLG SQNIGPEGPT VRTFINDFVK RELDNFLHRN PATADALKAR
IMQSERERKD IAGIKKLANE RAKKASLHNK KLRDCKIHFD DQHERRQDTT LFITEGDSAS
GSITKSRDVM TQAVFSLKGK PLNCFGLTKK VVYENEEFNL LQHALNIEDG IDGIRYNNIV
IATDADVDGM HIRLLLMTFF LQFFPDLVKA GHVSILQTPL FRVRNKKETI YCYSDEERRN
AIEKLGNKPE ITRFKGLGEI SPDEFGLFIG KDIRLDPVYL KDANIKGLLE YFMGKNTPDR
QQHIVNNLRI EKDDASINPT IEELVPVPVA V
//
