ID B3F5F5_STREQ Unreviewed; 621 AA.
AC B3F5F5;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 08-NOV-2023, entry version 83.
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:ABU96672.1};
OS Streptococcus dysgalactiae subsp. equisimilis (Streptococcus equisimilis).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=119602 {ECO:0000313|EMBL:ABU96672.1};
RN [1] {ECO:0000313|EMBL:ABU96672.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GGS M1 {ECO:0000313|EMBL:ABU96672.1}, and GGS M15
RC {ECO:0000313|EMBL:ABU96674.1};
RA Kosowska-Shick K., Strumbelj I., Seme K., McGhee P.L., Appelbaum P.C.;
RT "Molecular Characterization of Drug-resistant Streptococcus dysgalactiae
RT subsp. equisimilis Group G Strains Isolated in Slovenia.";
RL Submitted (MAY-2007) 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC {ECO:0000256|ARBA:ARBA00010708}.
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DR EMBL; EF619591; ABU96672.1; -; Genomic_DNA.
DR EMBL; EF619593; ABU96674.1; -; Genomic_DNA.
DR AlphaFoldDB; B3F5F5; -.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd16928; HATPase_GyrB-like; 1.
DR CDD; cd00822; TopoII_Trans_DNA_gyrase; 1.
DR CDD; cd03366; TOPRIM_TopoIIA_GyrB; 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 HAMAP; MF_01898; GyrB; 1.
DR InterPro; IPR002288; DNA_gyrase_B_C.
DR InterPro; IPR011557; GyrB.
DR InterPro; IPR003594; HATPase_C.
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 InterPro; IPR034160; TOPRIM_GyrB.
DR NCBIfam; TIGR01059; gyrB; 1.
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; PF00986; DNA_gyraseB_C; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
DR PRINTS; PR01159; DNAGYRASEB.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00387; HATPase_c; 1.
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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 429..543
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 621
FT /evidence="ECO:0000313|EMBL:ABU96672.1"
SQ SEQUENCE 621 AA; 68895 MW; 883DC174AA41B73A CRC64;
MIEENKHFEE KAQEYDASQI QVLEGLEAVR MRPGMYIGST AKEGLHHLVW EIVDNSIDEA
LAGFATHIQV FIEADNSITV VDNGRGIPVD IQAKTGRPAV ETVFTVLHAG GKFGGGGYKV
SGGLHGVGSS VVNALSTQLD VRVYKNGQIH YQEFKRGAVV ADLEVIGTTD VTGTTVHFTP
DPEIFTETTE FDYKVLAKRI QELAFLNRGL KISITDKRSG MEQEEHFHYE GGIGSYVEFL
NDKKDVIFET PIYTDGELEG IAVEVAMQYT TSYQETVMSF ANNIHTHEGG THEQGFRAAL
TRVINDYAKK NKILKENDDN LTGEDVREGL TAVISVKHPN PQFEGQTKTK LGNSEVVKIT
NRLFSEAFQR FLLENPQVAR KIVEKGILAS KARIAAKRAR EVTRKKSGWE ISNLPGKLAD
CSSNDASQNE LFIVEGDSAG GSAKSGRNRE FQAILPIRGK ILNVEKATMD KILANEEIRS
LFTAMGTGFG ADFDVSKARY QKLVIMTDAD VDGAHIRTLL LTLIYRFMRP VLEAGYVYIA
QPPIYGVKVG SEIKEYIQPG IEQEEQLKTA LEKYSVGRSK PTVQRYKGLG EMDDHQLWET
TMDPENRLMA RVTVDDAAEA D
//
