GYRB_ACICA
ID GYRB_ACICA Reviewed; 388 AA.
AC Q43947; Q59089; Q9ZA09;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 25-MAY-2022, entry version 96.
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 calcoaceticus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=471;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 23055 / DSM 30006 / CCUG 12804 / CIP 81.08 / LMD 22.16 / Delft
RC L360;
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 23055 / DSM 30006 / CCUG 12804 / CIP 81.08 / LMD 22.16 / Delft
RC L360;
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; AB008685; BAA75402.1; -; Genomic_DNA.
DR EMBL; D73427; BAA11152.1; -; Genomic_DNA.
DR EMBL; D73412; BAA11137.1; -; Genomic_DNA.
DR PIR; T43898; T43898.
DR AlphaFoldDB; Q43947; -.
DR SMR; Q43947; -.
DR STRING; 471.BUM88_19590; -.
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..>388
FT /note="DNA gyrase subunit B"
FT /id="PRO_0000145275"
FT DOMAIN 312..>388
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 12..14
FT /note="GVS -> RVG (in Ref. 2; BAA11152)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="E -> G (in Ref. 2; BAA11152)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="Y -> F (in Ref. 2; BAA11152)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 388
SQ SEQUENCE 388 AA; 43104 MW; 7DB9252E44FA17F0 CRC64;
DNSYKVSGGL HGVSVSVVNA LSSKLHLMIS RAGQVHEQEY QHGDPQYPLR VIGETDKSGT
TVRFWPSELT FTQTIFNVEI LARRLRELSF LNAGVRIVLR DERINLEHVY DYEGGLSEFV
KYINEGKTHL NEIFHFTADT DSGIGVEVAL QWNESYQENV RCFTNNIPQK DGGSHLAGFR
AALTRGLNQY LENENILKKE KVNVTGDDAR EGLTAIISVK VPDPKFSSQT KEKLVSSEVK
PAVEQAMNKE FSAYLLENPQ AAKSIAGKII DAARARDAAR KAREMTRRKS ALDIAGLPGK
LADCQEKDPA LSELYLVEGD SAGGSAKQGR NRKMQAILPL KGKILNVERA RFDKMISSQE
VGTLITALGC GIGREEYNPD KLRYHKII
