(data stored in ACNUC7421 zone)

SWISSPROT: D3EYQ9_CONWI

ID   D3EYQ9_CONWI            Unreviewed;       883 AA.
AC   D3EYQ9;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   30-AUG-2017, entry version 54.
DE   RecName: Full=DNA gyrase subunit A {ECO:0000256|HAMAP-Rule:MF_01897};
DE            EC=5.99.1.3 {ECO:0000256|HAMAP-Rule:MF_01897};
GN   Name=gyrA {ECO:0000256|HAMAP-Rule:MF_01897};
GN   OrderedLocusNames=Cwoe_0006 {ECO:0000313|EMBL:ADB48442.1};
OS   Conexibacter woesei (strain DSM 14684 / JCM 11494 / NBRC 100937 /
OS   ID131577).
OC   Bacteria; Actinobacteria; Thermoleophilia; Solirubrobacterales;
OC   Conexibacteraceae; Conexibacter.
OX   NCBI_TaxID=469383 {ECO:0000313|EMBL:ADB48442.1, ECO:0000313|Proteomes:UP000008229};
RN   [1] {ECO:0000313|Proteomes:UP000008229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14684 / JCM 11494 / NBRC 100937 / ID131577
RC   {ECO:0000313|Proteomes:UP000008229};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Mikhailova N., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Pukall R., Steenblock K.,
RA   Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Conexibacter woesei DSM 14684.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
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_01897}.
CC   -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining
CC       of double-stranded DNA. {ECO:0000256|HAMAP-Rule:MF_01897,
CC       ECO:0000256|SAAS:SAAS00846455}.
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_01897}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897}.
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_01897}.
CC   -!- SIMILARITY: Belongs to the topoisomerase GyrA/ParC subunit family.
CC       {ECO:0000256|HAMAP-Rule:MF_01897}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. {ECO:0000256|SAAS:SAAS00846457}.
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DR   EMBL; CP001854; ADB48442.1; -; Genomic_DNA.
DR   RefSeq; WP_012931495.1; NC_013739.1.
DR   STRING; 469383.Cwoe_0006; -.
DR   EnsemblBacteria; ADB48442; ADB48442; Cwoe_0006.
DR   KEGG; cwo:Cwoe_0006; -.
DR   eggNOG; ENOG4105C24; Bacteria.
DR   eggNOG; COG0188; LUCA.
DR   HOGENOM; HOG000076278; -.
DR   KO; K02469; -.
DR   OMA; THHWLLF; -.
DR   OrthoDB; POG091H025U; -.
DR   Proteomes; UP000008229; 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-HAMAP.
DR   GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-HAMAP.
DR   Gene3D; 1.10.268.10; -; 1.
DR   Gene3D; 3.30.1360.40; -; 1.
DR   Gene3D; 3.90.199.10; -; 1.
DR   HAMAP; MF_01897; GyrA; 1.
DR   InterPro; IPR024946; Arg_repress_C-like.
DR   InterPro; IPR005743; GyrA.
DR   InterPro; IPR006691; GyrA/parC_rep.
DR   InterPro; IPR035516; Gyrase/topoIV_suA_C.
DR   InterPro; IPR013760; Topo_IIA-like_dom.
DR   InterPro; IPR002205; Topo_IIA_A/C.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a.
DR   Pfam; PF03989; DNA_gyraseA_C; 6.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF101904; SSF101904; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3EYQ9.
DR   SWISS-2DPAGE; D3EYQ9.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00846465}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008229};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00846460};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00846445, ECO:0000313|EMBL:ADB48442.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00846452};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008229};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00846490}.
FT   DOMAIN       15    471       TOP4c. {ECO:0000259|SMART:SM00434}.
FT   COILED      443    477       {ECO:0000256|SAM:Coils}.
FT   MOTIF       532    538       GyrA-box. {ECO:0000256|HAMAP-Rule:
FT                                MF_01897}.
FT   ACT_SITE    126    126       O-(5'-phospho-DNA)-tyrosine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01897}.
SQ   SEQUENCE   883 AA;  97346 MW;  D4E01EAECC58CEF6 CRC64;
     MSATDQLSGG NIEPRALEEE MRSAYLDYAM SVIVGRALPD VRDGLKPVHR RVLFAMNEMG
     VQPNRPRAKS SRIVGEVMGK YHPHGDASIY DTLVRMAQDF SMRHLLVDGQ GNFGSVDDDP
     AAAMRYTEAR LARIATEMLR DIDADTVDFG PNYDGKNQEP LVLPARFPNL LVNGSSGIAV
     GMATNIPPHN LRETIAATIA YIENPEIDVD GLMQHIRGPD FPTGGIILGV GGIRDAYATG
     RGRVRVQARA HIEPLSQGKE AIVVTELPYQ VKKGGDGGLI QKIADLVHEK KIPEITDLRD
     ESDRHGMRFV IELKRDVLPK VVLNKLYKHT PMQTTFGVNM VALVDNVPKT LSLREVIGRY
     VDHQREVIVR RTKYELRRAE DRAHILEGLL IAQANIDEVI AIIRRSSDRE QARINLVNRF
     ELSERQAEAI LQMTLGRLTA LEVDKLRQEH ADLMERIREL REILGDEDRQ MAIIKEELQE
     ISDAYGNERR TAISYAEGEI DIEDLIADQQ MVITITKTGY IKSLPLATYR QQRRGGVGVT
     GMDMKDGDYI EHLFVTSTHD FLLFFTNRGK VYRSKVYELP EASRTAKGRA LVNILPLREG
     ERVQSVLSTR DFSEAPYLLF ATRKGTVKKT ELQAYNTPIK ADGIIAIKIR DDDELVAVRR
     VDEGDEVIIV SRAGLTVRFS EQDARSMGRD TSGVRGMDVG DSGEVIAMDI ARDDQDLLVI
     TENGFGKRTR IDEYRKTARG AKGVRTIRLT EARGGLAGAL VVREHQELVF ISQNGMVQRT
     GVRGINRYGR ASQGVKVMNV REDDSVRAIA LVVESDTAEA DEALELELGA DGVEGGGVVA
     VDADGAGADG GAPASDASDA PQGDDGDEPP ADGDSSSEGD AEV
//

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