ID Q9LCM4_MYCGO Unreviewed; 421 AA.
AC Q9LCM4;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 98.
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:BAA89744.1};
OS Mycobacterium gordonae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1778 {ECO:0000313|EMBL:BAA89744.1};
RN [1] {ECO:0000313|EMBL:BAA89744.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KPM 2201 {ECO:0000313|EMBL:BAA89744.1};
RX PubMed=10618105;
RA Kasai H., Ezaki T., Harayama S.;
RT "Differentiation of phylogenetically related slowly growing mycobacteria by
RT their gyrB sequences.";
RL J. Clin. Microbiol. 38:301-308(2000).
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; AB014191; BAA89744.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9LCM4; -.
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:BAA89744.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 345..421
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 115..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAA89744.1"
FT NON_TER 421
FT /evidence="ECO:0000313|EMBL:BAA89744.1"
SQ SEQUENCE 421 AA; 46465 MW; BDD161417CE9E553 CRC64;
GENSGYTVSG GLHGVGVSVV NALSTRLEVD IKRDGHEWSQ YYKRAVPGTL KQGETTRKTG
TTIRFWADPE IFETTQYDFE TVARRLQEMA FLNKGLTINL TDERVEQDEV VDEVVSDTAE
APKSAEEKAA ESKAPHKVKQ RTFHYPGGLV DFVKHINRTK SPIQQSVIDF EGKGTGHEVE
IAMQWNGGYS ESVHTFANTI NTHEGGTHEE GFRSALTSVV NKYAKDKKLL KEKDPNLTGD
DIREGLAAVI SVKVAEPQFE GQTKTKLGNT EVKSFVQKVC NEQLTHWFEA NPSEAKTVVN
KAVSSAQARI AARKARELVR RKSATDLGGL PGKLADCRST DPRKSELYVV EGDSAGGSAK
SGRDSMFQAI LPLRGKIINV EKARIDRVLK NTEVQAIITA LGTGIHDEFD ITKLRYHKIV
L
//
