GYRB1_ACILW
ID GYRB1_ACILW Reviewed; 390 AA.
AC Q44088; Q59125; Q9ZA00;
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 lwoffii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=28090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15309 / DSM 2403 / CCUG 33984 / JCM 6840 / NBRC 109760 / NCIMB
RC 12456 / NCTC 5866 / CIP 644.10;
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 290-389.
RC STRAIN=ATCC 15309 / DSM 2403 / CCUG 33984 / JCM 6840 / NBRC 109760 / NCIMB
RC 12456 / NCTC 5866 / CIP 644.10;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB008694; BAA75411.1; -; Genomic_DNA.
DR EMBL; D73434; BAA11159.1; -; Genomic_DNA.
DR EMBL; D73419; BAA11144.1; -; Genomic_DNA.
DR AlphaFoldDB; Q44088; -.
DR SMR; Q44088; -.
DR STRING; 28090.GCA_002119785_01163; -.
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..>390
FT /note="DNA gyrase subunit B"
FT /id="PRO_0000145279"
FT DOMAIN 313..>390
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 344
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 347
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT NON_TER 1
FT NON_TER 390
SQ SEQUENCE 390 AA; 43147 MW; 0BEC6AB97F6F989B CRC64;
DNSYKVSGGL HGVGVSVVNA LSEKLELTIH RAGKIHEQEY RHGDSQYPLK VVGDTNRTGT
RVRFWPSAET FSQTIFNVDI LARRLRELSF LNAGVRIVLR DERINAEHVF DYEGGLSEFV
KYINEGKTHL NDIFHFTAAQ ADNGITVEVA LQWNDSYQEN VRCFTNNIPQ KDGGTHLAGF
RAALTRGLNN YMDSENILKK EKVAVSGDDA REGLTAIVSV KVPDPKFSSQ TKEKLVSSEV
KTAVEQAMNK AFSEYLLENP QAAKAIAGKI IDAARARDAA RKAREMTRRK SALDIAGLPG
KLADCQEKDP ALSELYLVEG DSAGGSAKQG RNRKMQAILP LKGKILNVER ARFDRMISSA
EVGTLITALG CGIGREEYNP DKLRYHKIII
