ID G1UHM4_BACOV Unreviewed; 361 AA.
AC G1UHM4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
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:BAK82228.1};
OS Bacteroides ovatus.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=28116 {ECO:0000313|EMBL:BAK82228.1};
RN [1] {ECO:0000313|EMBL:BAK82228.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 5824 {ECO:0000313|EMBL:BAK82228.1};
RX PubMed=20118288; DOI=10.1099/ijs.0.021154-0;
RA Sakamoto M., Suzuki N., Benno Y.;
RT "hsp60 and 16S rRNA gene sequence relationships among species of the genus
RT Bacteroides with the finding that Bacteroides suis and Bacteroides tectus
RT are heterotypic synonyms of Bacteroides pyogenes.";
RL Int. J. Syst. Evol. Microbiol. 60:2984-2990(2010).
RN [2] {ECO:0000313|EMBL:BAK82228.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 5824 {ECO:0000313|EMBL:BAK82228.1};
RA Sakamoto M., Ohkuma M.;
RT "Identification and classification of the genus Bacteroides by multilocus
RT sequence analysis.";
RL Microbiology 157:3388-3397(2011).
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; AB619922; BAK82228.1; -; Genomic_DNA.
DR AlphaFoldDB; G1UHM4; -.
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 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 300..361
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAK82228.1"
FT NON_TER 361
FT /evidence="ECO:0000313|EMBL:BAK82228.1"
SQ SEQUENCE 361 AA; 40377 MW; 92081D4A506BD487 CRC64;
NALSTHMTTQ VFRDGKIYQQ EYEIGKPLYS VKEVGTADIT GTRQQFWPDN TIFTETVYDY
KILASRLREL AYLNAGLRIT LTDRRVVNED GSFKGEQFYS EEGLREFVRF IESSREHLIN
DVIYLNSEKQ GIPIEVAIMY NTGFSENVHS YVNNINTIEG GTHLAGFRRA LTRTLKKYAE
DSKMLEKVKV EISGDDFREG LTAVISVKVA EPQFEGQTKT KLGNNEVMGA VDQAVGEVLA
YYLEEHPKEA KTIVDKVILA ATARHAARKA REMVQRKSPM SGGGLPGKLA DCSDKDPSKC
ELFLVEGDSA GGTAKQGRNR MFQAILPLRG KILNVEKAMY HKALESDEIR NIYTALGVTI
G
//
