ID Q0ZP91_VIBCL Unreviewed; 384 AA.
AC Q0ZP91;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=DNA gyrase subunit B {ECO:0000256|ARBA:ARBA00019166};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
DE Flags: Fragment;
OS Vibrio cholerae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=666 {ECO:0000313|EMBL:ABC47934.1};
RN [1] {ECO:0000313|EMBL:ABC47934.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=510 {ECO:0000313|EMBL:ABC47934.1};
RA Hou X.-L., Cao Q.-Y., Chen Z.;
RT "Classification and Identification of Enteropathogenic Bacteria Prevalent
RT in China Based on gyrB Gene.";
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABC47934.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=510 {ECO:0000313|EMBL:ABC47934.1};
RX PubMed=17302148;
RA Hou X.L., Cao Q.Y., Pan J.C., Chen Z.;
RT "Classification and identification of vibrio cholerae and vibrio
RT parahaemolyticus isolates based on gyrB gene phylogenetic analysis.";
RL Wei Sheng Wu Xue Bao 46:884-889(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}.
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DR EMBL; DQ316972; ABC47934.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0ZP91; -.
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 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.
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 310..384
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABC47934.1"
FT NON_TER 384
FT /evidence="ECO:0000313|EMBL:ABC47934.1"
SQ SEQUENCE 384 AA; 42366 MW; 8B86E3758469147C CRC64;
KVSGGLHGVG VSVVNALSEK VLLTIYRGGK IHSQTYHHGV PQAPLAVVGE TERTGTTVRF
WPSAQTFTNI EFHYDILAKR LRELSFLNSG VSIKLTDERE EDKKDHFMYE GGIQAFVTHL
NRNKTPIHEK VFHFNQERED GISVEVAMQW NDGFQENIYC FTNNIPQRDG GTHLAGFRGA
LTRTLNNYMD KEGFSKKAQA ATSGDDAREG LTAVVSVKVP DPKFSSQTKD KLVSSEVKSA
VESAMNEKLA DFLAENPSEA KNVCSKIIDA ARAREAARKA REMTRRKGAL DLAGLPGKLA
DCQEKDPALS ELYIVEGDSA GGSAKQGRNR KNQAILPLKG KILNVEKARF DKMLSSQEVA
TLITALGCGI GRDEYNPDKL RYHN
//
