ID I0R0M0_9MICO Unreviewed; 684 AA.
AC I0R0M0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=IMCC13023_09590 {ECO:0000313|EMBL:EIC91406.1};
OS Candidatus Aquiluna sp. IMCC13023.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Luna cluster; Luna-1 subcluster; Aquiluna.
OX NCBI_TaxID=1081644 {ECO:0000313|EMBL:EIC91406.1, ECO:0000313|Proteomes:UP000054510};
RN [1] {ECO:0000313|Proteomes:UP000054510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC13023 {ECO:0000313|Proteomes:UP000054510};
RX PubMed=22689238; DOI=10.1128/JB.00586-12;
RA Kang I., Lee K., Yang S.J., Choi A., Kang D., Lee Y.K., Cho J.C.;
RT "Genome sequence of "Candidatus Aquiluna" sp. strain IMCC13023, a marine
RT member of the Actinobacteria isolated from an arctic fjord.";
RL J. Bacteriol. 194:3550-3551(2012).
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 -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC {ECO:0000256|ARBA:ARBA00010708}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIC91406.1}.
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; AJKR01000003; EIC91406.1; -; Genomic_DNA.
DR RefSeq; WP_007541862.1; NZ_AJKR01000003.1.
DR AlphaFoldDB; I0R0M0; -.
DR STRING; 1081644.IMCC13023_09590; -.
DR PATRIC; fig|1081644.3.peg.969; -.
DR eggNOG; COG0187; Bacteria.
DR Proteomes; UP000054510; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd16928; HATPase_GyrB-like; 1.
DR CDD; cd00822; TopoII_Trans_DNA_gyrase; 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:SF1; DNA GYRASE SUBUNIT B, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:EIC91406.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054510};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 460..574
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 684 AA; 74407 MW; 62503AC0B1AAAC6B CRC64;
MDDYSARHLS VLEGLEAVRK RPGMYIGSTD GRGLMHCLWE IIDNSVDEAL AGHGKRIGVV
IHTDGSITVQ DDGRGVPVDI EPRTGLSGVE VVFTKLHAGG KFGGGSYGAS GGLHGVGASV
VNALSSRLDV EVDRAGQTWA MSFHRGEPGV FASEGPAADF TPFVDKSELR VVGKVTKSKT
GTRVRYWPDS QIFEPGADFQ MQDLESRLRQ TAFLVPGLVL SVHDELSDVS QEFVFEGGIT
EYVEYLAADG PVLATRRINE TTSFRETVPV LDEASGSMKS KEVERQCVVD VALRWGSGFD
TRVKSFVNII STPKGGSHLT GFEQALLKSF RTAIEANARR LKATSLKIER DDVMAGLTAV
VSVSFPEPQF EGQTKETLGT PAIKAIVANS VAKWADELLA GKIRGTKAEV DALLDKVVSE
AKTRISARSL KDTQRRKNAL ESSSLPSKLV DCRGSATVGS ELFIVEGDSA LGTAKLARDS
AFQALLPIRG KILNVQKASL SDMLSNAECA AIIQVLGAGS GRTFDLEQVR YEKIILMSDA
DVDGAHIRTL LLTLFFRYMR PLVEAGRVYA AVPPLHRVET AGRNKEVIYT YSQQELNDLL
RSLEKAGKSY KQPIQRYKGL GEMDADQLAE TTMQPSNRML RRITAVDAAA GERTFELLMG
NEVAPRRDFI VDSADDFDRE KIDA
//
