(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZJS1_PSEAB

ID   A0A0H2ZJS1_PSEAB        Unreviewed;       806 AA.
AC   A0A0H2ZJS1;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 17.
DE   RecName: Full=DNA gyrase subunit B {ECO:0000256|HAMAP-Rule:MF_01898, ECO:0000256|SAAS:SAAS00746468};
DE            EC=5.99.1.3 {ECO:0000256|HAMAP-Rule:MF_01898, ECO:0000256|SAAS:SAAS00470646};
GN   Name=gyrB {ECO:0000256|HAMAP-Rule:MF_01898,
GN   ECO:0000313|EMBL:ABJ14960.1};
GN   OrderedLocusNames=PA14_00050 {ECO:0000313|EMBL:ABJ14960.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ14960.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ14960.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ14960.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- FUNCTION: A type II topoisomerase that negatively supercoils
CC       closed circular double-stranded (ds) DNA in an ATP-dependent
CC       manner to modulate DNA topology and maintain chromosomes in an
CC       underwound state. Negative supercoiling favors strand separation,
CC       and DNA replication, transcription, recombination and repair, all
CC       of which involve strand separation. Also able to catalyze the
CC       interconversion of other topological isomers of dsDNA rings,
CC       including catenanes and knotted rings. Type II topoisomerases
CC       break and join 2 DNA strands simultaneously in an ATP-dependent
CC       manner. {ECO:0000256|HAMAP-Rule:MF_01898}.
CC   -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining
CC       of double-stranded DNA. {ECO:0000256|HAMAP-Rule:MF_01898,
CC       ECO:0000256|SAAS:SAAS00470725}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00609977};
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.
CC       In the heterotetramer, GyrA contains the active site tyrosine that
CC       forms a transient covalent intermediate with DNA, while GyrB binds
CC       cofactors and catalyzes ATP hydrolysis. {ECO:0000256|HAMAP-
CC       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
CC       topoisomerases; in organisms with a single type II topoisomerase
CC       this enzyme also has to decatenate newly replicated chromosomes.
CC       {ECO:0000256|HAMAP-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; CP000438; ABJ14960.1; -; Genomic_DNA.
DR   RefSeq; WP_003097268.1; NC_008463.1.
DR   ProteinModelPortal; A0A0H2ZJS1; -.
DR   SMR; A0A0H2ZJS1; -.
DR   EnsemblBacteria; ABJ14960; ABJ14960; PA14_00050.
DR   KEGG; pau:PA14_00050; -.
DR   KO; K02470; -.
DR   OMA; DCSSRDP; -.
DR   Proteomes; UP000000653; 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-HAMAP.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-HAMAP.
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; -; 1.
DR   HAMAP; MF_01898; GyrB; 1.
DR   InterPro; IPR002288; DNA_gyrase_B_C.
DR   InterPro; IPR011557; GyrB.
DR   InterPro; IPR003594; HATPase_C.
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.
DR   InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR   InterPro; IPR013759; Topo_IIA_cen_dom.
DR   InterPro; IPR018522; TopoIIA_CS.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034160; TOPRIM_GyrB.
DR   PANTHER; PTHR10169; PTHR10169; 1.
DR   Pfam; PF00204; DNA_gyraseB; 1.
DR   Pfam; PF00986; DNA_gyraseB_C; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   PRINTS; PR00418; TPI2FAMILY.
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; 2.
DR   TIGRFAMs; TIGR01059; gyrB; 1.
DR   PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0H2ZJS1.
DR   SWISS-2DPAGE; A0A0H2ZJS1.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00528655};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01898};
KW   DNA-binding {ECO:0000256|SAAS:SAAS00709661};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00107007};
KW   Magnesium {ECO:0000256|SAAS:SAAS00058309};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00058330};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00528653};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00528650}.
FT   DOMAIN      420    535       Toprim. {ECO:0000259|PROSITE:PS50880}.
SQ   SEQUENCE   806 AA;  90189 MW;  DD85D2321F471A57 CRC64;
     MSENNTYDSS SIKVLKGLDA VRKRPGMYIG DTDDGTGLHH MVFEVVDNSI DEALAGYCSE
     ISITIHTDES ITVRDNGRGI PVDIHKEEGV SAAEVIMTVL HAGGKFDDNT YKVSGGLHGV
     GVSVVNALSH ELRLTIRRHN KVWEQVYHHG VPQFPLREVG ETDGSGTEVH FKPSPETFSN
     IHFSWDILAK RIRELSFLNS GVGILLRDER TGKEELFKYE GGLKAFVEYL NTNKTAVNEV
     FHFNVQREED GVGVEVALQW NDSFNENLLC FTNNIPQRDG GTHLAGFRSA LTRNLNNYIE
     AEGLAKKFKI ATTGDDAREG LTAIISVKVP DPKFSSQTKD KLVSSEVKTA VEQEMGKYFA
     DFLLENPNEA KAVVGKMIDA ARAREAARKA REMTRRKGAL DIAGLPGKLA DCQEKDPALS
     ELYIVEGDSA GGSAKQGRNR RTQAILPLKG KILNVEKARF DKMLSSQEVG TLITALGCGI
     GREEYNIDKL RYHNIIIMTD ADVDGSHIRT LLLTFFFRQM PELIERGYIY IAQPPLYKVK
     RGKQEQYIKD DQAMEEYMTQ SALEDASLHV NEHAPGLSGA ALEKLVNEYR GVIATLKRLS
     RLYPQELTEH FIYLPTVSVD DLANESAMQG WLEKFQARLT AAEKSGLTYK ASLREDRERH
     LWLPEVELVA HGLSSYVTFN RDFFASNDYR SVSLLGDQLN SLLEDGAYVQ KGERKRPISA
     FKDGLDWLMA EGTKRHSIQR YKGLGEMNPE QLWETTMDPN VRRMLKVTIE DAIAADQIFN
     TLMGDAVEPR RDFIESNALA VSNLDV
//

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