ID J7I2U2_AERSO Unreviewed; 338 AA.
AC J7I2U2;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
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:AFQ20537.1};
OS Aeromonas sobria.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=646 {ECO:0000313|EMBL:AFQ20537.1};
RN [1] {ECO:0000313|EMBL:AFQ20537.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=XX-67 {ECO:0000313|EMBL:AFQ20537.1};
RX PubMed=22725694; DOI=10.1111/j.1472-765X.2012.03281.x;
RA Hu M., Wang N., Pan Z.H., Lu C.P., Liu Y.J.;
RT "Identity and virulence properties of Aeromonas isolates from diseased
RT fish, healthy controls and water environment in China.";
RL Lett. Appl. Microbiol. 55:224-233(2012).
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; JX025831; AFQ20537.1; -; Genomic_DNA.
DR AlphaFoldDB; J7I2U2; -.
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:AFQ20537.1"
FT NON_TER 338
FT /evidence="ECO:0000313|EMBL:AFQ20537.1"
SQ SEQUENCE 338 AA; 37576 MW; A8050AFC6F39DB82 CRC64;
LLLTIRRNGH VYEQTYHLGE PLAPLKQIGD SSSGTGTEVR FWPSPTIFTD TLYHYEILAK
RLRELSFLNS GVSIRLQDER DGREVHFCYE GGIKAFVEYL NQNKTPIHPK VFHFSTEQDG
IGVEVAMQWN DAYQEGVYCF TNNIPQRDGG THLVGFRTAL TRTLNTYMDK EDYSKKAKSA
ASGDDVREGL IAVISVKVPD PKFSSQTKDK LVSSEVKTAV EQAMGEKLGE FLLENPGDAK
IVVNKIIDAA RAREAARKAR ELTRRKGALD IAGLPGKLAD CQEKDPALSE LYIVEGDSAG
GSAKQGRNRK NQAILPLKGK ILNVEKARFD KMISSQEV
//
