ID A0A132MQX1_9ACTN Unreviewed; 1258 AA.
AC A0A132MQX1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=LI90_1430 {ECO:0000313|EMBL:KWW99791.1};
OS Carbonactinospora thermoautotrophica.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Carbonactinosporaceae; Carbonactinospora.
OX NCBI_TaxID=1469144 {ECO:0000313|EMBL:KWW99791.1, ECO:0000313|Proteomes:UP000070188};
RN [1] {ECO:0000313|Proteomes:UP000070188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H1 {ECO:0000313|Proteomes:UP000070188};
RA MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA Chang R., Ford T., Nguyen P.Q., Woodward J., Permingeat H., Joshi N.S.,
RA Silver P.A., Usadel B., Rutherford A.W., Friesen M., Prell J.;
RT "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT of multiple isolates of Streptomyces thermoautotrophicus.";
RL Submitted (APR-2015) 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 -!- 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:KWW99791.1}.
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DR EMBL; LAXD01000001; KWW99791.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A132MQX1; -.
DR STRING; 1469144.LI90_1430; -.
DR PATRIC; fig|1469144.10.peg.1570; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000070188; 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:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR CDD; cd16928; HATPase_GyrB-like; 1.
DR CDD; cd00081; Hint; 2.
DR CDD; cd00093; HTH_XRE; 1.
DR CDD; cd00822; TopoII_Trans_DNA_gyrase; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.670; -; 2.
DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.10.28.10; Homing endonucleases; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR002288; DNA_gyrase_B_C.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR003586; Hint_dom_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_2.
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 NCBIfam; TIGR01443; intein_Cterm; 1.
DR NCBIfam; TIGR01445; intein_Nterm; 1.
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; PF14890; Intein_splicing; 1.
DR Pfam; PF14528; LAGLIDADG_3; 1.
DR Pfam; PF01751; Toprim; 1.
DR PRINTS; PR01159; DNAGYRASEB.
DR PRINTS; PR00379; INTEIN.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SMART; SM00433; TOP2c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR SUPFAM; SSF55608; Homing endonucleases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 2.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:KWW99791.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein splicing {ECO:0000256|ARBA:ARBA00023000};
KW Reference proteome {ECO:0000313|Proteomes:UP000070188};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 861..998
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 1085..1109
FT /note="Intein C-terminal splicing"
FT /evidence="ECO:0000259|PROSITE:PS50818"
SQ SEQUENCE 1258 AA; 139434 MW; 4E9FB05A9DCB6DEF CRC64;
MTAQTTALLA GGEPDPSNYT ARHLLVLEGL EAVRKRPGMY IGSTDSRGLM HCLWEIIDNA
VDEALAGFCD RIDVLLYRDG SVEVRDNGRG IPVDIEPKTG LSGVEVVMTK LHAGGKFGGG
SYAASGGLHG VGASVVNALS ARLDVEVDRD GATHAMSFRR GVPGEFAGDG PNAAFEARSG
LRKIKRVAKR VTGTRVRFWP DRQIFLKDAG FSLEDLYNRA RQTAFLVPGL TIAVRDERGE
ETVEETFCFA GGISEFCEFL APDRPVTDVL RFSGTGTFVE TVPVLDEKGH LTPADVEREL
TVDVALRWGT EYDTVVRSFV NIIATPKGGT HVQGFERALV RVLNDQARAV RLLRANDEPL
TKDDVLEGLT AVVTVRLAEP QFEGQTKEVL GTPAASRIVT QVVSQQLKAF LTSTKRNDKA
QARAVLEKVV SAARTRIAAR QHKETQRRKN ALETSALPAK LADCRSDDVE RSELFIVEGD
SALGTAKLAR NSEFQALLPI RGKILNVQKA SVTDMLKNAE CAAIIQVIGA GSGRSFDINQ
ARYGKVVLMS VAPDEPVLFT DRDGRFVLRR IGPAVDAEIE AAGLGELDGT VSVDLVARQP
RVSPVKQFIR HHHKGLMYRI KTVYGRSVNV TGGHSVFTFE NGELTLKPAS ELRVGDLAVA
PRQLPRPVEP QEELDLALLL KRSGQDHAIR IEGEAVRRLM VQKIAARQPS YLRRDEERVR
LPQEVWARLA AVRKTRGITL ADMACRLGYR QACSISEFET CRSLPPASVF TRYLAELDEP
WPAEAEKVPA LVDQWAASPD TARNARYRGT SQATWLADLD ETDLAWLAAE PDGRDVVLYP
RAHRADTVNR YLPVTEDLCY MLGWYLAEGS CSASSRLSFS LGANDEPYLP ELMAVIERVT
GRRAVLARSE RFPGSRHVYV QAPLFVRLVR ALGMGGRAHE KRLPDLVLNC REEHQLAFLE
GYYLGDGTKY VDGRAVVFAT SSRELADGLL YLLGQLGVLA SIHDRGAYEF EIRGSKVETK
SSYLISVASR DSLQKLRRLW RRTACAEGFE RRISEGWSKS VYTPISDTLI GLPIKEIEVT
EYDSDVYDLS VPEDENFISG TGGLLTHNTD ADVDGAHIRC LLLTLFYRYM RPMIEAGRVY
AAVPPLHRIE VIGNGRRRNE YVYTYSDNEM KRVVADLLKR GKKIKEPIQR YKGLGEMDAD
QLAETTMDPR RRTLRRITIA DAEVAERMFE LLMGNEVAPR RDFITQSASL LDRSRIDT
//
