ID H9BYX2_9FUSO Unreviewed; 176 AA.
AC H9BYX2;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
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:AFD96384.1};
OS Pseudostreptobacillus hongkongensis.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Pseudostreptobacillus.
OX NCBI_TaxID=1162717 {ECO:0000313|EMBL:AFD96384.1};
RN [1] {ECO:0000313|EMBL:AFD96384.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HKU34 {ECO:0000313|EMBL:AFD96384.1};
RA Woo P.C.Y., Wu A.K.L., Tsang C.C., Leung K.-W., Curreem S.O., Lee R.A.,
RA Lau S.K.P.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFD96384.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HKU34 {ECO:0000313|EMBL:AFD96384.1};
RX PubMed=24912824; DOI=10.1099/ijs.0.061242-0;
RA Woo P.C., Wu A.K., Tsang C.C., Leung K.W., Ngan A.H., Curreem S.O.,
RA Lam K.W., Chen J.H., Chan J.F., Lau S.K.;
RT "Streptobacillus hongkongensis sp. nov., isolated from patients with quinsy
RT and septic arthritis, and emended descriptions of the genus Streptobacillus
RT and Streptobacillus moniliformis.";
RL Int. J. Syst. Evol. Microbiol. 64:3034-3039(2014).
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; JQ087400; AFD96384.1; -; Genomic_DNA.
DR AlphaFoldDB; H9BYX2; -.
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 Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
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; 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 100..176
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFD96384.1"
FT NON_TER 176
FT /evidence="ECO:0000313|EMBL:AFD96384.1"
SQ SEQUENCE 176 AA; 19371 MW; 3567C76336399BF6 CRC64;
LVCVISLKFP EPQFESQTKS KLGSSEAIGV VSGILSNKLK MYLEDNPKEA NIIVDKIAIS
KEAREAAKKA REMVTKKSSF EVGSLPGKLA DCSSKNPEES EIFIVEGDSA GGSAKQGRNR
MFQAILPLRG KILNVEKANE HRILESSEIK AMITAFGTGF ADRFDIEKLR YHKIII
//