(data stored in SCRATCH zone)

SWISSPROT: A0KEE9_AERHH

ID   A0KEE9_AERHH            Unreviewed;       803 AA.
AC   A0KEE9;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   11-DEC-2019, entry version 111.
DE   RecName: Full=DNA gyrase subunit B {ECO:0000256|HAMAP-Rule:MF_01898};
DE            EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_01898};
GN   Name=gyrB {ECO:0000256|HAMAP-Rule:MF_01898,
GN   ECO:0000313|EMBL:ABK37959.1};
GN   OrderedLocusNames=AHA_0004 {ECO:0000313|EMBL:ABK37959.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / JCM
OS   1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK37959.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK37959.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.,
RA   Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA   Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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. {ECO:0000256|HAMAP-
CC       Rule:MF_01898}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|HAMAP-Rule:MF_01898,
CC         ECO:0000256|SAAS:SAAS01220860};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00612567};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00709652};
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|HAMAP-Rule:MF_01898}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01898}.
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. {ECO:0000256|HAMAP-
CC       Rule:MF_01898}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01898}.
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DR   EMBL; CP000462; ABK37959.1; -; Genomic_DNA.
DR   RefSeq; WP_011704050.1; NC_008570.1.
DR   RefSeq; YP_854532.1; NC_008570.1.
DR   SMR; A0KEE9; -.
DR   STRING; 380703.AHA_0004; -.
DR   EnsemblBacteria; ABK37959; ABK37959; AHA_0004.
DR   GeneID; 4490516; -.
DR   KEGG; aha:AHA_0004; -.
DR   PATRIC; fig|380703.7.peg.5; -.
DR   eggNOG; ENOG4105C7D; Bacteria.
DR   eggNOG; COG0187; LUCA.
DR   HOGENOM; HOG000075155; -.
DR   KO; K02470; -.
DR   OMA; LWETTMH; -.
DR   BioCyc; AHYD380703:G1G7B-4-MONOMER; -.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd03366; TOPRIM_TopoIIA_GyrB; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   Gene3D; 3.40.50.670; -; 2.
DR   HAMAP; MF_01898; GyrB; 1.
DR   InterPro; IPR002288; DNA_gyrase_B_C.
DR   InterPro; IPR011557; GyrB.
DR   InterPro; IPR041423; GyrB_insert.
DR   InterPro; IPR003594; HATPase_C.
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   InterPro; IPR034160; TOPRIM_GyrB.
DR   Pfam; PF00204; DNA_gyraseB; 1.
DR   Pfam; PF00986; DNA_gyraseB_C; 1.
DR   Pfam; PF18053; GyrB_insert; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00433; TOP2c; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
DR   TIGRFAMs; TIGR01059; gyrB; 1.
DR   PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0KEE9.
DR   SWISS-2DPAGE; A0KEE9.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00528655};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01898};
KW   DNA-binding {ECO:0000256|SAAS:SAAS00709661};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01898, ECO:0000256|SAAS:SAAS00470744,
KW   ECO:0000313|EMBL:ABK37959.1}; Magnesium {ECO:0000256|SAAS:SAAS00445358};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00445373};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00528653};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00528650}.
FT   DOMAIN          418..533
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   803 AA;  89492 MW;  6DCC5A6FFC95F8F4 CRC64;
     MSENTYDSSN IKVLKGLDAV RKRPGMYIGD TDDGSGLHHM VFEVVDNSID EALAGYCSDI
     QVKIHSDGSV SVRDNGRGIP VDIHPEEGRS AAEVIMTVLH AGGKFDDNSY KVSGGLHGVG
     VSVVNALSDK LLLTIRRNGH VYEQTYHLGE PQAPLKQIGD STGTGTEVRF WPSPTIFSDT
     LFHYEILAKR LRELSFLNSG VSIRLLDERD GREAHFCYEG GIKAFVEYLN QNKTPIHPKV
     FHFTTEQDGI GVEVAMQWND AYQEGVYCFT NNIPQRDGGT HLVGFRTALT RTLNSYMDKE
     DYSKKAKSAA SGDDVREGLI AVISVKVPDP KFSSQTKDKL VSSEVKTAVE QAMGEKLADF
     LLENPGDAKI VVNKIIDAAR AREAARKARE LTRRKGALDI AGLPGKLADC QEKDPALSEL
     YIVEGDSAGG SAKQGRNRKN QAILPLKGKI LNVEKARFDK MISSQEVGTL ITALGCGIGR
     DEYNPDKLRY HNIIIMTDAD VDGAHIRTLL LTFFYRQMPE IIERGYVYIA QPPLYKVKKG
     KQEQYLKDED ALLQYQTAMA LDGATLHVNE SAPAIGGEAL ERLVNQHRSV SHLITRMSRR
     APEAVLTQLI YQPELNEALL SSESDLLAWC QSMEAVLNES NHGIQYQMQV RHDEERRLFV
     PHAVVRQHGV DREYPLSYDF LQSSEYRQLV SLGKEIANLI EEGGYIKRGE KVKPVASFVE
     AVEWLMGEGK RGIYIQRYKG LGEMNPDQLW ETTMDPEARR MLRVTIDDAV GADQLFSTLM
     GDAVEPRRDF IETNALRVAN LDV
//

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