ID M5B5S1_9PSED Unreviewed; 374 AA.
AC M5B5S1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
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:CCE21657.1};
OS Pseudomonas sp. R-42085.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1095398 {ECO:0000313|EMBL:CCE21657.1};
RN [1] {ECO:0000313|EMBL:CCE21657.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R-42085 {ECO:0000313|EMBL:CCE21657.1};
RX PubMed=23333025; DOI=10.1016/j.syapm.2012.11.007;
RA Ghyselinck J., Velivelli S.L., Heylen K., O'Herlihy E., Franco J.,
RA Rojas M., De Vos P., Prestwich B.D.;
RT "Bioprospecting in potato fields in the Central Andean Highlands: Screening
RT of rhizobacteria for plant growth-promoting properties.";
RL Syst. Appl. Microbiol. 36:116-127(2013).
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; HE603573; CCE21657.1; -; Genomic_DNA.
DR AlphaFoldDB; M5B5S1; -.
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 304..374
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CCE21657.1"
FT NON_TER 374
FT /evidence="ECO:0000313|EMBL:CCE21657.1"
SQ SEQUENCE 374 AA; 41226 MW; B82A309D2C999D0C CRC64;
GLHGVGVSVV NALSEELVLT VRRSGKIWEQ TYVHGVPQAP MAIVGDSETT GTQIHFKASS
ETFKNIHFSW DILAKRIREL SFLNSGVGIV LKDERSGKEE LFKYEGGLRA FVEYLNTNKT
AVNQVFHFNV QREDGIGVEI ALQWNDSFNE NLLCFTNNIP QRDGGTHLVG FRSALTRNLN
TYIEQEGLAK KHKVATTGDD AREGLTAIIS VKVPDPKFSS QTKDKLVSSE VKTAVEQEMG
KYFSDFLLEN PNEAKLVVGK MIDAARAREA ARKAREMTRR KGALDIAGLP GKLADCQEKD
PALSELYLVE GDSAGGSAKQ GRNRRTQAIL PLKGKILNVE KARFDKMISS QEVGTLITAL
GCGIGREEYN IDKL
//
