ID Q7WVR3_CAMJU Unreviewed; 405 AA.
AC Q7WVR3;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, 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:AAP97533.1};
OS Campylobacter jejuni subsp. jejuni.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=32022 {ECO:0000313|EMBL:AAP97533.1};
RN [1] {ECO:0000313|EMBL:AAP97533.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NLEP02-8197 {ECO:0000313|EMBL:AAP97533.1};
RA Munro C.K., Price L., Moses J., Moterrassed A., Woodward D.L.;
RT "Phylogenetic analysis of Campylobacter jejuni, Campylobacter coli and
RT Campylobacter lari using DNA sequence comparisons of DNA gyrase subunit B
RT gene.";
RL Submitted (JUN-2003) 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}.
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DR EMBL; AY330118; AAP97533.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7WVR3; -.
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 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 319..405
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAP97533.1"
FT NON_TER 405
FT /evidence="ECO:0000313|EMBL:AAP97533.1"
SQ SEQUENCE 405 AA; 44941 MW; B074B37318B1D1A4 CRC64;
VLHAGGKFDK DTYKVSGGLH GVGVSVVNAL SKKLVATVER NGEIYRQEFS EGKVISEFGV
IGKSKKTGTT IEFWPDDQIF EVTEFDYEIL AKRFRELAYL NPKITINFKD NRVGKHESFH
FEGGISQFVT DLNKKEALTK AIFFSVDEED VNVEVALLYN DTYSENLLSF VNNIKTPDGG
THETGFRMGL TRVISNYIEA NASAREKDNK ITGDDVREGL IAVVSVKVPE PQFEGQTKGK
LGSTYVRPIV SKASFEYLTK YFEENPIEAK AIMNKALIAA RGREAAKKAR ELTRKKESLS
VGTLPGKLAD CQSKDPSESE IYLVEGDSAG GSAKQGRERS FQAILPLRGK ILNVEKARLD
KILKSEQIQN MITAFGCGIG EDFDLSKLRY HKIIIMTDAD VDGSH
//
