ID Q2A6X9_9MICO Unreviewed; 370 AA.
AC Q2A6X9;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 04-APR-2006, sequence version 1.
DT 24-JAN-2024, entry version 69.
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:CAJ57494.1};
OS Microbacterium lacticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=33885 {ECO:0000313|EMBL:CAJ57494.1};
RN [1] {ECO:0000313|EMBL:CAJ57494.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type strain: DSM 20427 {ECO:0000313|EMBL:CAJ57494.1};
RX PubMed=16684595; DOI=10.1016/j.syapm.2006.04.001;
RA Richert K., Brambilla E., Stackebrandt E.;
RT "The phylogenetic significance of peptidoglycan types: Molecular analysis
RT of the genera Microbacterium and Aureobacterium based upon sequence
RT comparison of gyrB, rpoB, recA and ppk and 16SrRNA genes.";
RL Syst. Appl. Microbiol. 30:102-108(2007).
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; AM181488; CAJ57494.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2A6X9; -.
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: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 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 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.
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 Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 104..277
FT /note="DNA topoisomerase type IIA subunit B"
FT /evidence="ECO:0000259|Pfam:PF00204"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAJ57494.1"
FT NON_TER 370
FT /evidence="ECO:0000313|EMBL:CAJ57494.1"
SQ SEQUENCE 370 AA; 41328 MW; 862FB51134879B76 CRC64;
IRRQGFVWRQ SFAGGGKPQA PLAQGEETVE TGTVITFWPD AEIFETVDFD YDTLRTRFQQ
TAFLNKGLRI TLSDLRPSSA YVVDTEDGQS VERQPHDEFH YERGLVDYVE YLNKIRKADV
VNDEIIEVEA EDTVRHISLE LAMQWTTSYT ENVFTFANTI NTHEGGTHEE GFRAAMTTYI
NKYAREKGLL KEKDDNLTGD DIREGLTAVI SVKLSEPQFE GQTKTKLGNT EAKAFVQKVV
GDQLTDWLDR NPVQAKRVIM KAVDAATARL AARKARETAR RKSVFESASM PEKLKDCTSK
DPSISEIFLV EGDSAGGSAV SGRDPERQAI LSLRGKILNV EKARLDRALG NTEIQAMISA
FGTGIGEDFD
//