ID Q9S5H6_ACISP Unreviewed; 303 AA.
AC Q9S5H6;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 24-JAN-2024, entry version 85.
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:BAA75440.1};
OS Acinetobacter sp.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=472 {ECO:0000313|EMBL:BAA75440.1};
RN [1] {ECO:0000313|EMBL:BAA75440.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CIP 64.2 {ECO:0000313|EMBL:BAA75440.1};
RX PubMed=10028249;
RA Yamamoto S., Bouvet P.J.M., Harayama S.;
RT "Phylogenetic structures of the genus Acinetobacter based on gyrB
RT sequences: comparison with the grouping by DNA-DNA hybridization.";
RL Int. J. Syst. Bacteriol. 49:87-95(1999).
CC -!- FUNCTION: A type II topoisomerase that negatively supercoils closed
CC circular double-stranded (ds) DNA in an ATP-dependent manner to
CC modulate DNA topology and maintain chromosomes in an underwound state.
CC Negative supercoiling favors strand separation, and DNA replication,
CC transcription, recombination and repair, all of which involve strand
CC separation. Also able to catalyze the interconversion of other
CC topological isomers of dsDNA rings, including catenanes and knotted
CC rings. Type II topoisomerases break and join 2 DNA strands
CC simultaneously in an ATP-dependent manner.
CC {ECO:0000256|ARBA:ARBA00001978}.
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 -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains. In
CC the heterotetramer, GyrA contains the active site tyrosine that forms a
CC transient covalent intermediate with DNA, while GyrB binds cofactors
CC and catalyzes ATP hydrolysis. {ECO:0000256|ARBA:ARBA00011234}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC {ECO:0000256|ARBA:ARBA00010708}.
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DR EMBL; AB008723; BAA75440.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9S5H6; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:BAA75440.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 115..284
FT /note="DNA topoisomerase type IIA subunit B"
FT /evidence="ECO:0000259|Pfam:PF00204"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAA75440.1"
FT NON_TER 303
FT /evidence="ECO:0000313|EMBL:BAA75440.1"
SQ SEQUENCE 303 AA; 33473 MW; 59EAD8BC89405D6A CRC64;
DNSYKVSGGL HGVGVSVVNA LSKKLHLTIH RAGQVHEQEY AHGDPQYPLK VVGETDTSGT
TVRFWPSELT FSQTIFSVDI LARRLRELSF LNAGVRIVLR DERVNLEHVY DYEGGLSEFV
KYINEGKTHL NEIFHFTTDA DNGIGVEVAL QWNDSYQENV RCFTNNIPQK DGGTHLAGFR
AALTRGLNSY MENESLLKKE KVAVTGDDAR EGLTAIISVK VPDPKFSSQT KEKLVSSEVK
PAVEQAMNKE FSAYLLENPQ AAKSIAGKII DAARARDAAR KAREMTRRKS ALDIAGLPGK
LAD
//