ID E1CAD7_9MYCO Unreviewed; 419 AA.
AC E1CAD7;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
DE Flags: Fragment;
GN Name=gyrB {ECO:0000313|EMBL:BAJ22236.1};
OS Mycolicibacterium moriokaense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=39691 {ECO:0000313|EMBL:BAJ22236.1};
RN [1] {ECO:0000313|EMBL:BAJ22236.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 6375 {ECO:0000313|EMBL:BAJ22236.1};
RA Kasai H., Harayama S.;
RT "Construction of the gyrB database for identification and classification of
RT High GC Gram positive bacteria.";
RL Submitted (MAY-1998) 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 -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC {ECO:0000256|ARBA:ARBA00010708}.
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DR EMBL; AB014292; BAJ22236.1; -; Genomic_DNA.
DR AlphaFoldDB; E1CAD7; -.
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:0006265; P:DNA topological change; IEA:InterPro.
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; 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; PF01751; Toprim; 1.
DR PRINTS; PR01159; DNAGYRASEB.
DR PRINTS; PR00418; TPI2FAMILY.
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:BAJ22236.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 343..419
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 114..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAJ22236.1"
FT NON_TER 419
FT /evidence="ECO:0000313|EMBL:BAJ22236.1"
SQ SEQUENCE 419 AA; 45854 MW; A89B3CE58BD361A6 CRC64;
EGAYSVSGGL HGVGVSVVNA LSTRLEADIC TDGYEWFQTY DNSIPGTLKQ GEKTKKTGTT
IRFWADPNVF ETTNYDFETV ARRLQEMAFL NKGLTITLSD ERVTADEVTD EVVSDTAEAP
KSAEEKAAEA AGPHKVKHRT FHYPGGLVDF VKHINRTKSP IHQSIVDFSG KGEGHEVEIA
LQWNAGYSES VHTFANTINT HEGGTHEEGF RAALTSVVNK YAKDKKLLKD KDPNLTGDDI
REGLAAVISV KVAEPQFEGQ TKTKLGNTEV KSFVQKICNE QLSHWFEANP AEAKTVVNKA
VSSAQARIAA RKARELVRRK SATDIGGLPG KLADCRSTDP RKSELYVVEG DSAGGSAKSG
RDSMFQAILP LRGKIINVEK ARIDRVLKNT EVQAIITALG TGIHDEFDIS KLRYHKIVL
//
