ID A0A255H303_9ACTN Unreviewed; 701 AA.
AC A0A255H303;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-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=CGZ93_08795 {ECO:0000313|EMBL:OYO22011.1};
OS Enemella dayhoffiae.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Enemella.
OX NCBI_TaxID=2016507 {ECO:0000313|EMBL:OYO22011.1, ECO:0000313|Proteomes:UP000216311};
RN [1] {ECO:0000313|EMBL:OYO22011.1, ECO:0000313|Proteomes:UP000216311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML 130396 {ECO:0000313|EMBL:OYO22011.1,
RC ECO:0000313|Proteomes:UP000216311};
RA Bernier A.-M., Bernard K., Domingo M.-C.;
RT "Draft whole genome sequences of clinical Proprionibacteriaceae strains.";
RL Submitted (JUL-2017) 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:OYO22011.1}.
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DR EMBL; NMVQ01000012; OYO22011.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255H303; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000216311; 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: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:OYO22011.1};
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:UP000216311};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 475..589
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 701 AA; 76536 MW; F3A5D5819D4EE22A CRC64;
MSETATQSSS RTAKKTGAVG HDYEARHLLV LEGLEAVRKR PAMYIGSTDT KGLMHCLWEI
IDNAVDEALS GFGTEIEVVL AKDGSIKVTD HARGIPVDVE PRTGLSGVEV VFTKLHAGGK
FGAGSYNATG GLHGVGASVV NALSSRLDVE VDRSSTTWGM SFKHGIPGTF DGEGPNAKFT
PGGGLQKLGR AKRGATGTRV RYWPDRQIFL KDAALSLESL TGRARQTSFL VPGLAISVRD
ERGNEVVEEV HRHDGGISEF CEFLAADQPL TEVIRLQGRD EFTETVPMLD DNGSLTPTDV
DRDVEVDIAL RWGHGYDTTT KSFVNIIATP KGGTHVAGYE RAMTKALSKA LEGTRLLKSG
EEIVKDDVLE GLTSVVTVRL AEPQFEGQTK EVLGTPAVSR LVAKVVEREL GDFLSSNKAA
VKHQARTVLE KVVSASRTRV QARAHKEAQR RKNALESSTL PAKLKDCRSN DVDKCELFIV
EGDSALGTAQ RARNSEYQAL LPIRGKILNV QKASVGDMLK NAECSSIIQV VGGGSGRTFE
LDAVRYGKII FMADADSDGA HIRTLLATLF FKYMRPLLEA GRVYTAVPPL HRFEITNPRK
GMEKYLYTYS DAEYQRKTAE LTKKNIAFKE PQRYKGLGEM DADQLKETTM SPLHRTLRRM
TVDDAAVAET TFEMLMGNEV APRKEFIVDG AYAIDAEQID A
//