ID Q59JF2_STRCB Unreviewed; 300 AA.
AC Q59JF2;
DT 26-APR-2005, integrated into UniProtKB/TrEMBL.
DT 26-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 74.
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:BAD91444.1};
OS Streptococcus canis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1329 {ECO:0000313|EMBL:BAD91444.1};
RN [1] {ECO:0000313|EMBL:BAD91444.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GTC 423 {ECO:0000313|EMBL:BAD91444.1};
RA Kawamura Y., Itoh Y., Mishima N., Ohkusu K., Kasai H., Ezaki T.;
RT "High genetic similarity of Streptococcus agalactiae and Streptococcus
RT difficilis: S. difficilis Eldar et al. 1995 is a later synonym of S.
RT agalactiae Lehmann and Neumann 1896 (Approved Lists 1980).";
RL Int. J. Syst. Evol. Microbiol. 55:961-965(2005).
RN [2] {ECO:0000313|EMBL:BAE97466.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GTC 423 Type {ECO:0000313|EMBL:BAE97466.1};
RX PubMed=16487673; DOI=10.1016/j.syapm.2005.12.003;
RA Itoh Y., Kawamura Y., Kasai H., Shah M.M., Nhung P.H., Yamada M., Sun X.,
RA Koyana T., Hayashi M., Ohkusu K., Ezaki T.;
RT "dnaJ and gyrB gene sequence relationship among species and strains of
RT genus Streptococcus.";
RL Syst. Appl. Microbiol. 29:368-374(2006).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB175046; BAD91444.1; -; Genomic_DNA.
DR EMBL; AB236191; BAE97466.1; -; Genomic_DNA.
DR AlphaFoldDB; Q59JF2; -.
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; 3.30.565.10; 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; IPR000565; Topo_IIA_B.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
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 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.
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 118..287
FT /note="DNA topoisomerase type IIA subunit B"
FT /evidence="ECO:0000259|Pfam:PF00204"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAD91444.1"
FT NON_TER 300
FT /evidence="ECO:0000313|EMBL:BAD91444.1"
SQ SEQUENCE 300 AA; 33336 MW; 8CED7B1FCD34D476 CRC64;
GGGYKVSGGL HGVGSSVVNA LSTQLDVRVY KNGQIHYQEF KRGAVVADLA VIGTTDTTGT
TVHFTPDPEI FAETTEFDYK VLAKRIQELA FLNRGLKISI TDKRLGMKQE EHFHYEGGIG
SYVEFLNDKK DVIFNTPIYT DGELDGVAVE VAMQYTTSYH ETVMSFANNI HTHEGGTHEQ
GFRTALTRVI NDYAKKNKIL KENDDNLTGE DVREGLTAVI SVKHPNPQFE GQTKTKLGNS
EVVKITNRLF SEAFQRFLLE NPQVARKIVE KGILASKARI AAKRAREVTR KKSGLEISNL
//
