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Database: UniProt
Entry: D7UTE0_9PSED
LinkDB: D7UTE0_9PSED
Original site: D7UTE0_9PSED 
ID   D7UTE0_9PSED            Unreviewed;       375 AA.
AC   D7UTE0;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 53.
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:BAJ10899.1};
OS   Pseudomonas flexibilis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=706570 {ECO:0000313|EMBL:BAJ10899.1};
RN   [1] {ECO:0000313|EMBL:BAJ10899.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 14085 {ECO:0000313|EMBL:BAJ10899.1};
RX   PubMed=20817837; DOI=10.1099/ijs.0.024612-0;
RA   Hirota K., Yamahira K., Nakajima K., Nodasaka Y., Okuyama H., Yumoto I.;
RT   "Pseudomonas toyotomiensis sp. nov., a psychrotolerant facultative
RT   alkaliphile that utilizes hydrocarbons.";
RL   Int. J. Syst. Evol. Microbiol. 61:1842-1848(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; AB571150; BAJ10899.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7UTE0; -.
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          302..375
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAJ10899.1"
FT   NON_TER         375
FT                   /evidence="ECO:0000313|EMBL:BAJ10899.1"
SQ   SEQUENCE   375 AA;  41221 MW;  DA66C91AEA49C009 CRC64;
     GVGVSVVNAL SEELVMTIRR AGKVWEQTYV HGVPQAPLAA VGETEGTGTQ IHFKPSAQTF
     RNIHFSWDIL AKRLRELSFL NSGVGIVLRD ERSGKEELFK YEGGLKAFVE YLNTNKTAVN
     SVFHFTVQRE EDGVGVEVAL QWNDGFNENI LCFTNNIPQR DGGTHLAGFR SALTRNLNNY
     IEAEGLAKKF KISTTGDDAR EGLTAIISVK VPDPKFSSQT KDKLVSSEVK TAVEQEMGKF
     FADFLLENPN DAKAVVGKMI DAARAREAAR KAREMTRRKG ALDIAGLPGK LADCQEKDPA
     LSELYLVEGD SAGGSAKQGR NRRTQAILPL KGKILNVEKA RFDKMLSSQE VGTLITALGC
     GIGRDEYNID KLRYH
//
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