ID   GYRB_ACIVR              Reviewed;         216 AA.
AC   Q44277; Q60168;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=DNA gyrase subunit B;
DE            EC=5.6.2.2 {ECO:0000255|PROSITE-ProRule:PRU00995};
DE   Flags: Fragments;
GN   Name=gyrB;
OS   Acinetobacter venetianus (strain ATCC 31012 / DSM 23050 / BCRC 14357 / CCUG
OS   45561 / CIP 110063 / KCTC 2702 / LMG 19082 / RAG-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1191460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8934907; DOI=10.1099/00207713-46-2-506;
RA   Yamamoto S., Harayama S.;
RT   "Phylogenetic analysis of Acinetobacter strains based on the nucleotide
RT   sequences of gyrB genes and on the amino acid sequences of their
RT   products.";
RL   Int. J. Syst. Bacteriol. 46:506-511(1996).
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:0000250|UniProtKB:P0AES6}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00995};
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:0000250|UniProtKB:P0AES6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0AES6}.
CC   -!- MISCELLANEOUS: Few gyrases are as efficient as E.coli at forming
CC       negative supercoils. Not all organisms have 2 type II topoisomerases;
CC       in organisms with a single type II topoisomerase this enzyme also has
CC       to decatenate newly replicated chromosomes.
CC       {ECO:0000250|UniProtKB:P0AES6}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC       {ECO:0000305}.
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DR   EMBL; D73440; BAA11165.1; -; Genomic_DNA.
DR   EMBL; D73425; BAA11150.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q44277; -.
DR   SMR; Q44277; -.
DR   eggNOG; COG0187; Bacteria.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   Gene3D; 3.30.565.10; -; 1.
DR   Gene3D; 3.40.50.670; -; 1.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR001241; Topo_IIA.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR   InterPro; IPR013759; Topo_IIA_B_C.
DR   InterPro; IPR018522; TopoIIA_CS.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   Pfam; PF01751; Toprim; 1.
DR   SMART; SM00433; TOP2c; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
DR   PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; DNA-binding; Isomerase; Nucleotide-binding;
KW   Topoisomerase.
FT   CHAIN           <1..>216
FT                   /note="DNA gyrase subunit B"
FT                   /id="PRO_0000145285"
FT   DOMAIN          140..>216
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT   SITE            171
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT   SITE            174
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT   NON_CONS        116..117
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         216
SQ   SEQUENCE   216 AA;  23872 MW;  C73D4B3B7A7A6484 CRC64;
     SYKVSGGLHG VGVSVVNALS KKLHLTIHRA GQIHEQEYAH GDPQYPLKVV GETDTSGTTV
     RFWPSELTFS QTIFSVDILA RRLRELSFLN AGVRIVLRDE RVNLEHIYDY EVGLSEKSAL
     DIAGLPGKLA DCQEKDPALS ELYLVEGDSA GGSAKQGRNR KMQAILPLKG KILNVERARF
     DKMISSQEVG TLITALGCGI GREEYNPDKL RYHKII