ID D4NWJ6_VIBSP Unreviewed; 234 AA.
AC D4NWJ6;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 44.
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:ADD64542.1};
OS Vibrio splendidus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=29497 {ECO:0000313|EMBL:ADD64542.1};
RN [1] {ECO:0000313|EMBL:ADD64542.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=0407CG136 {ECO:0000313|EMBL:ADD64542.1};
RX PubMed=21873482; DOI=10.1128/AEM.00665-11;
RA Preheim S.P., Timberlake S., Polz M.F.;
RT "Merging taxonomy with ecological population prediction in a case study of
RT vibrionaceae.";
RL Appl. Environ. Microbiol. 77:7195-7206(2011).
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; GU378473; ADD64542.1; -; Genomic_DNA.
DR AlphaFoldDB; D4NWJ6; -.
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 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 46..216
FT /note="DNA topoisomerase type IIA subunit B"
FT /evidence="ECO:0000259|Pfam:PF00204"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADD64542.1"
FT NON_TER 234
FT /evidence="ECO:0000313|EMBL:ADD64542.1"
SQ SEQUENCE 234 AA; 26174 MW; 2BC9D8449FB1CBDD CRC64;
FTNIEFHYDI LAKRLRELSF LNSGVSIKLI DKREEDKMDH FEYEGGIQAF VEHLNTNKTP
IIQKIFHFDH EREDGITVEV AMQWNDGYQE NIYCFTNNIP QRDGGAHLAG FRGALTRTLN
SFMDKEGFSK KAKTSTSGDD AREGLTAIVS VKVPDPKFSS QTKDKLVSSE VKSAVESTMG
EKLSEFLIEN PGEAKIVCSK IIDAARARDA ARKAREMTRR KGALDLAGLP GKLA
//