ID   GYRB_ACIJO              Reviewed;         389 AA.
AC   Q44081; Q59123; Q9ZA02;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=DNA gyrase subunit B;
DE            EC=5.6.2.2 {ECO:0000255|PROSITE-ProRule:PRU00995};
DE   Flags: Fragment;
GN   Name=gyrB;
OS   Acinetobacter johnsonii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=40214;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 17909 / DSM 6963 / CCUG 19095 / NCTC 10308 / CIP 64.6 / B8;
RX   PubMed=10028249; DOI=10.1099/00207713-49-1-87;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-118 AND 289-388.
RC   STRAIN=ATCC 17909 / DSM 6963 / CCUG 19095 / NCTC 10308 / CIP 64.6 / B8;
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; AB008692; BAA75409.1; -; Genomic_DNA.
DR   EMBL; D73433; BAA11158.1; -; Genomic_DNA.
DR   EMBL; D73418; BAA11143.1; -; Genomic_DNA.
DR   PIR; T43905; T43905.
DR   AlphaFoldDB; Q44081; -.
DR   SMR; Q44081; -.
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; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   Gene3D; 3.40.50.670; -; 1.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR001241; Topo_IIA.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
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   Pfam; PF00204; DNA_gyraseB; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   SMART; SM00433; TOP2c; 1.
DR   SUPFAM; SSF54211; SSF54211; 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..>389
FT                   /note="DNA gyrase subunit B"
FT                   /id="PRO_0000145277"
FT   DOMAIN          312..>389
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT   SITE            343
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT   SITE            346
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT   CONFLICT        99
FT                   /note="L -> W (in Ref. 2; BAA11158)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         389
SQ   SEQUENCE   389 AA;  43033 MW;  1057835FB422154F CRC64;
     DNSYKVSGGL HGVGVSVVNA LSRKLELTIH RAGHIHQQEY KHGDPVYPLT VVGDTDTTGT
     TVRFWPSAET FSQTIFNVDI LARRLRELSF LNAGVRIVLR DERIHAEHVF DYEGGLSEFV
     KYINQGKTHL NDIFHFTVQA ENGIGVEVAL QWNDTYQENV RCFTNNIPQK DGGTHLAGFR
     AALTRGLNSY MENENLLKKE KVAVSGDDAR EGLTAIVSVK VPDPKFSSQT KEKLVSSEVK
     PAVEQAMNKS FSEYLLENPQ AAKSIAGKII DAARARDAAR KAREMTRRKS ALDIAGLPGK
     LADCQEKDPA LSELYLVEGD SAGGSAKQGR NRKMQAILPL KGKILNVERA RFDKMISSQE
     VGTLITALGC GIGREEYNPD KLRYHKIII