ID Q5GQ73_LEIXC Unreviewed; 351 AA.
AC Q5GQ73;
DT 01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 80.
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:CAH04912.1};
OS Leifsonia xyli subsp. cynodontis (Clavibacter xyli cynodontis).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=31966 {ECO:0000313|EMBL:CAH04912.1};
RN [1] {ECO:0000313|EMBL:CAH04912.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 46306 {ECO:0000313|EMBL:CAH04912.1};
RX PubMed=15567231; DOI=10.1016/j.mimet.2004.09.004;
RA Richert K., Brambilla E., Stackebrandt E.;
RT "Development of PCR primers specific for the amplification and direct
RT sequencing of gyrB genes from microbacteria, order Actinomycetales.";
RL J. Microbiol. Methods 60:115-123(2005).
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; AJ784797; CAH04912.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5GQ73; -.
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 292..351
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAH04912.1"
FT NON_TER 351
FT /evidence="ECO:0000313|EMBL:CAH04912.1"
SQ SEQUENCE 351 AA; 38921 MW; 7FF00E4939EF51C2 CRC64;
SYRNGVPQAP LEQGEETEAT GTTIVFWPSP ETFETVEFDY DTLRTRFQQM AFLNKGLRIA
ITDQRTALGS LEGQVDEESE PRGEVFLYEK GLTDYVHYLN AAKKAEVVHD EIISFELEDT
DRKIALEVAM QWTTSYNESV FTYANTINTH EGGTHEEGFR AALTTLVNRY AREKNILKDK
DDNLSGDDVR EGLTAVISVK LSEPQFEGQT KTKLGNTEAK AFVQKVVGDQ LADWFDRNPN
QAKEIIRKAL QAATARIVAR KARETARRKG LLESGGMPGK LKDCQSKDPT LSEIFIVEGD
SAGGSAVQGR NPETQAILPL RGKILNVEKA RLDRALANNE VQAMITAFGA G
//
