ID Q2A6W7_9MICO Unreviewed; 362 AA.
AC Q2A6W7;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 04-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 72.
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:CAJ57506.1};
OS Microbacterium thalassium.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=362649 {ECO:0000313|EMBL:CAJ57506.1};
RN [1] {ECO:0000313|EMBL:CAJ57506.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type strain: DSM 12511 {ECO:0000313|EMBL:CAJ57506.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM181500; CAJ57506.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2A6W7; -.
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 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 305..362
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAJ57506.1"
FT NON_TER 362
FT /evidence="ECO:0000313|EMBL:CAJ57506.1"
SQ SEQUENCE 362 AA; 40363 MW; 94F3CE4CFE97AC7F CRC64;
VEVRRQGHVW RQSYQGGGIP IAPLAQGETS SDTGTTITFW PDEGIFDTVD FDYDTLRTRF
QQMAFLNKGL RIDLRDERAL EVLDAVEEAA EPEVRHDSFL YERGLVDYVG YLNKVRHADA
VNDEIIDFES EDTERKIAME MAMQWTTSYT ENVFTFANTI NTHEGGTHEE GFRAALTALV
NRYARANNLL KDKDDNLTGE DIREGLTAVI SVKLSEPQFE GQTKTKLGNT EAKAFVQKVV
GDQLGDWFDR NPAQAKNIIR KAIDAASARL AARKARETAR RKSVFESAAM PDKLKDCTSK
DPSISEIFLV EGDSAGGSAV QGRDPHTQAI LALRGKILNV ERARLDKALS NKEVQAMIQA
FG
//
