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Database: UniProt
Entry: A0A1A3BDN4_9MYCO
LinkDB: A0A1A3BDN4_9MYCO
Original site: A0A1A3BDN4_9MYCO 
ID   A0A1A3BDN4_9MYCO        Unreviewed;       409 AA.
AC   A0A1A3BDN4;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=A5663_08590 {ECO:0000313|EMBL:OBI72017.1};
OS   Mycobacterium sp. E740.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1834149 {ECO:0000313|EMBL:OBI72017.1, ECO:0000313|Proteomes:UP000092151};
RN   [1] {ECO:0000313|Proteomes:UP000092151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E740 {ECO:0000313|Proteomes:UP000092151};
RA   Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Sam S., Sreng N.,
RA   Him V., Kerleguer A., Cheng S.;
RL   Submitted (JUN-2016) 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}.
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:OBI72017.1}.
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DR   EMBL; LZKP01000215; OBI72017.1; -; Genomic_DNA.
DR   RefSeq; WP_068153631.1; NZ_LZKP01000215.1.
DR   AlphaFoldDB; A0A1A3BDN4; -.
DR   STRING; 1834149.A5663_08590; -.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000092151; 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: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   Gene3D; 3.30.230.10; -; 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; IPR000565; Topo_IIA_B.
DR   InterPro; IPR013506; Topo_IIA_bsu_dom2.
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   PRINTS; PR01159; DNAGYRASEB.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092151};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          238..397
FT                   /note="DNA topoisomerase type IIA subunit B"
FT                   /evidence="ECO:0000259|Pfam:PF00204"
SQ   SEQUENCE   409 AA;  45619 MW;  981163EFF91E5E11 CRC64;
     MKQFSSGWPI CGKCCEVAYF PWLGGAHRCD VTSRDDWPDY DFFEWEDDSF ESRPFDDFRY
     EDGLHRLLWD VIAHSAEVAA SAVSVTLRAD GGVEVSHDGR DPNLDGAIAA LQDNFLSELA
     CRTAFPDLAA AYVEEPSERN SLPARLDIEI HRDGFIWFQR YDCGVARLVE CRGATTKTGV
     TVRCWPESLV CEMTDGDAGA ALKRLQRMAF LREGLTIDVV DDRRTRPARS RTFCYPGGLV
     DYCRFLTRIS MPLHDNVIQL SGRRRGFAVE IAMRWTTGYS PTIQVFDTFS GSPRPSAHEE
     AIAHAVTATV AGPVKQHVAD RIPLPAAVPD LTTRDIAEGL TAVVNVRHRA SPPEDERPSP
     EVVSIIYTLC HRHLAGWLDA NPRAADLIAD KAIAGHHYAR MPRRSFCRG
//
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