ID C4TJ47_9GAMM Unreviewed; 338 AA.
AC C4TJ47;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=DNA gyrase subunit B {ECO:0000256|ARBA:ARBA00019166};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
DE Flags: Fragment;
GN Name=gyrB {ECO:0000313|EMBL:BAH66720.1};
OS Aeromonas sp. KYO1080.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=582246 {ECO:0000313|EMBL:BAH66720.1};
RN [1] {ECO:0000313|EMBL:BAH66720.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KYO1080 {ECO:0000313|EMBL:BAH66720.1};
RA Tateyama S., Ogura Y., Matsuoka H., Takeda N., Nakayama K., Ooka T.,
RA Shimada M., Saeki Y., Setoyama M., Hayashi T.;
RT "Phylogroup and virulence-related phenotypes highly associated with
RT invasive diseases of Aeromonas spp.";
RL Submitted (DEC-2008) 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}.
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; AB473107; BAH66720.1; -; Genomic_DNA.
DR AlphaFoldDB; C4TJ47; -.
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 289..338
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAH66720.1"
FT NON_TER 338
FT /evidence="ECO:0000313|EMBL:BAH66720.1"
SQ SEQUENCE 338 AA; 37573 MW; F3C4145F179C461C CRC64;
QLLLTIRRNG HVYEQTYHLG EPQAPLKQIG DSTGTGTEVR FWPSPTIFSD TLFHYEILAK
RLRELSFLNS GVSIRLLDER DGREAHFCYE GGIKAFVEYL NQNKTPIHPK VFHFTTEQDG
IGVEVAMQWN DAYQEGVYCF TNNIPQRDGG THLVGFRTAL TRTLNSYMDK EDYSKKAKSA
ASGDDVREGL IAVISVKVPD PKFSSQTKDK LVSSEVKTAV EQAMGEKLAD FLLENPGDAK
IVVNKIIDAA RAREAARKAR ELTRRKGALD IAGLPGKLAD CQEKDPALSE LYIVEGDSAG
GSAKQGRNRK NQAILPLKGK ILNVEKARFD KMISSQEV
//