ID I0B8U9_9GAMM Unreviewed; 372 AA.
AC I0B8U9;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
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 Pseudoalteromonas luteoviolacea.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=43657 {ECO:0000313|EMBL:AFH58796.1};
RN [1] {ECO:0000313|EMBL:AFH58796.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM6061 {ECO:0000313|EMBL:AFH58796.1};
RX PubMed=23015771; DOI=10.3390/md10081729;
RA Vynne N.G., Mansson M., Gram L.;
RT "Gene sequence based clustering assists in dereplication of
RT Pseudoalteromonas luteoviolacea strains with identical inhibitory activity
RT and antibiotic production.";
RL Mar. Drugs 10:1729-1740(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; JQ280430; AFH58796.1; -; Genomic_DNA.
DR AlphaFoldDB; I0B8U9; -.
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 302..372
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFH58796.1"
FT NON_TER 372
FT /evidence="ECO:0000313|EMBL:AFH58796.1"
SQ SEQUENCE 372 AA; 41330 MW; 9DCCB18FD81AB748 CRC64;
VGVSVVNALS EKLQLTIRRD GQVHQQKYTM GVPDAPLAVI GEAESTGTEL RFWPSPETFS
DINFHYDILA KRLRELSFLN SGVSIILTDE REENKQDHFK YEGGIQAFVE YLNRKKTPVH
QSVFHFTTER EDGISVEVSM QWNDGFQENI YCFTNNIPQR DGGTHLAGFR AALTRTLNTY
MEKEGFNKKN KTSATGDDAR EGLTAVVSVK VPDPKFSSQT KDKLVSSEVK GAVEQAMAEK
LNEFLLENPQ DAKTVVNKIV DAARAREAAR KAREMTRRKG VMDLAGLPGK LADCQEKDPA
LSELYIVEGD SAGGSAKQGR NRKNQAILPL KGKILNVEKA RFDKMLSSQE VATLITALGC
GIGRDEYDPE KL
//
